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- EMDB-19720: RNA polymerase II early elongation complex bound to TFIIE and TFI... -

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Basic information

Entry
Database: EMDB / ID: EMD-19720
TitleRNA polymerase II early elongation complex bound to TFIIE and TFIIF - state b (composite structure)
Map dataComposite map for EC14b (sharpened)
Sample
  • Complex: RNA polymerase II early elongation complex bound to TFIIE and TFIIF - state b
    • Complex: RNA polymerase II
      • Protein or peptide: x 12 types
    • Complex: DNA and RNA
      • DNA: x 2 types
      • RNA: x 1 types
    • Complex: Transcription factor IIE subunit 1 and Transcription factor IIF
      • Protein or peptide: x 3 types
  • Ligand: x 2 types
KeywordsRNA polymerase II / promoter escape / de novo transcription / TRANSCRIPTION
Function / homology
Function and homology information


transcription factor TFIIE complex / phosphatase activator activity / transcription open complex formation at RNA polymerase II promoter / TFIIF-class transcription factor complex binding / B-WICH complex positively regulates rRNA expression / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / RNA Polymerase I Transcription Termination / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter ...transcription factor TFIIE complex / phosphatase activator activity / transcription open complex formation at RNA polymerase II promoter / TFIIF-class transcription factor complex binding / B-WICH complex positively regulates rRNA expression / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / RNA Polymerase I Transcription Termination / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / Formation of RNA Pol II elongation complex / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes / mRNA Capping / mRNA Splicing - Major Pathway / mRNA Splicing - Minor Pathway / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Elongation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Pol II CTD phosphorylation and interaction with CE / Estrogen-dependent gene expression / transcription factor TFIIF complex / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / nuclear lumen / Abortive elongation of HIV-1 transcript in the absence of Tat / FGFR2 alternative splicing / RNA polymerase II general transcription initiation factor binding / : / Viral Messenger RNA Synthesis / Signaling by FGFR2 IIIa TM / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / mRNA Splicing - Minor Pathway / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / Processing of Capped Intron-Containing Pre-mRNA / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RNA polymerase II activity / organelle membrane / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / transcription-coupled nucleotide-excision repair / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / RNA polymerase I complex / transcription by RNA polymerase I / RNA polymerase III complex / transcription by RNA polymerase III / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / translation initiation factor binding / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / mRNA Splicing - Major Pathway / DNA-directed RNA polymerase complex / negative regulation of protein binding / promoter-specific chromatin binding / transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / DNA-templated transcription initiation / positive regulation of transcription elongation by RNA polymerase II / TP53 Regulates Transcription of DNA Repair Genes / response to virus / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / microtubule cytoskeleton / cell junction / protein phosphatase binding / Estrogen-dependent gene expression / transcription by RNA polymerase II / chromosome, telomeric region / nucleic acid binding / protein dimerization activity / molecular adaptor activity / nuclear speck
Similarity search - Function
Transcription factor TFIIE alpha subunit, C-terminal / C-terminal general transcription factor TFIIE alpha / Transcription initiation factor IIE subunit alpha, N-terminal / Transcription factor TFE/TFIIEalpha HTH domain / TFIIEalpha/SarR/Rpc3 HTH domain / Transcription factor E / TFIIE alpha subunit / TFE/IIEalpha-type HTH domain profile. / Transcription initiation factor IIE / Transcription initiation factor IIF, beta subunit ...Transcription factor TFIIE alpha subunit, C-terminal / C-terminal general transcription factor TFIIE alpha / Transcription initiation factor IIE subunit alpha, N-terminal / Transcription factor TFE/TFIIEalpha HTH domain / TFIIEalpha/SarR/Rpc3 HTH domain / Transcription factor E / TFIIE alpha subunit / TFE/IIEalpha-type HTH domain profile. / Transcription initiation factor IIE / Transcription initiation factor IIF, beta subunit / TFIIF beta subunit, HTH domain / TFIIF, beta subunit, N-terminal / TFIIF, beta subunit HTH domain / TFIIF, beta subunit N-terminus / Transcription initiation factor IIF, alpha subunit / Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) / Transcription Factor IIF, Rap30/Rap74, interaction / Zinc finger, TFIIB-type / TFIIB zinc-binding / DNA-directed RNA polymerase II subunit Rpb4-like / RNA polymerase Rpb4/RPC9, core / DNA-directed RNA-polymerase II subunit / RNA polymerase II, heptapeptide repeat, eukaryotic / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1 C-terminal repeat / Eukaryotic RNA polymerase II heptapeptide repeat. / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 superfamily / RNA polymerase Rpb1, domain 7 / Rpb4/RPC9 superfamily / Pol II subunit B9, C-terminal zinc ribbon / RNA polymerase RBP11 / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Zinc finger TFIIS-type signature. / RNA polymerase subunit Rpb7-like / HRDC-like superfamily / RNA polymerase Rpb7-like , N-terminal / RNA polymerase Rpb7-like, N-terminal domain superfamily / SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / DNA-directed RNA polymerase, M/15kDa subunit / RNA polymerases M/15 Kd subunit / RNA polymerase subunit 9 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10 / RNA polymerases N / 8 kDa subunit / RNA polymerases N / 8 Kd subunits signature. / DNA-directed RNA polymerase M, 15kDa subunit, conserved site / RNA polymerases M / 15 Kd subunits signature. / DNA-directed RNA polymerase subunit/transcription factor S / RNA polymerase, Rpb8 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / RNA polymerase Rpb8 / RNA polymerase subunit 8 / RNA polymerase, Rpb5, N-terminal / RNA polymerase Rpb5, N-terminal domain superfamily / RNA polymerase Rpb5, N-terminal domain / DNA-directed RNA polymerase, subunit RPB6 / DNA-directed RNA polymerase subunit Rpo11 / DNA directed RNA polymerase, 7 kDa subunit / RNA polymerase archaeal subunit P/eukaryotic subunit RPABC4 / RNA polymerase, subunit H/Rpb5, conserved site / RNA polymerases H / 23 Kd subunits signature. / RNA polymerase subunit CX / DNA-directed RNA polymerase Rpb11, 13-16kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / RNA polymerases L / 13 to 16 Kd subunits signature. / Zinc finger, TFIIS-type / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / DNA-directed RNA polymerase, 30-40kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 / RNA polymerases D / 30 to 40 Kd subunits signature. / DNA-directed RNA polymerase, RBP11-like dimerisation domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerase, subunit H/Rpb5 C-terminal / RNA polymerase subunit RPABC4/transcription elongation factor Spt4 / RPB5-like RNA polymerase subunit superfamily / RNA polymerase Rpb5, C-terminal domain / Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit / DNA-directed RNA polymerase, 14-18kDa subunit, conserved site / RNA polymerases K / 14 to 18 Kd subunits signature. / Ribosomal protein S1-like RNA-binding domain / S1 RNA binding domain / S1 domain / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RNA polymerase Rpb1, clamp domain superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb1, domain 3
Similarity search - Domain/homology
RNA polymerase II subunit D / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase subunit / RNA polymerase II subunit K / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit beta ...RNA polymerase II subunit D / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase subunit / RNA polymerase II subunit K / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit E / General transcription factor IIF subunit 2 / General transcription factor IIE subunit 1 / General transcription factor IIF subunit 1 / DNA-directed RNA polymerase II subunit RPB9
Similarity search - Component
Biological speciesSus scrofa (pig) / unidentified adenovirus / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsZhan Y / Grabber F / Oberbeckmann E / Dienemann C / Cramer P
Funding support Germany, 1 items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: Mol Cell / Year: 2024
Title: Three-step mechanism of promoter escape by RNA polymerase II.
Authors: Yumeng Zhan / Frauke Grabbe / Elisa Oberbeckmann / Christian Dienemann / Patrick Cramer /
Abstract: The transition from transcription initiation to elongation is highly regulated in human cells but remains incompletely understood at the structural level. In particular, it is unclear how ...The transition from transcription initiation to elongation is highly regulated in human cells but remains incompletely understood at the structural level. In particular, it is unclear how interactions between RNA polymerase II (RNA Pol II) and initiation factors are broken to enable promoter escape. Here, we reconstitute RNA Pol II promoter escape in vitro and determine high-resolution structures of initially transcribing complexes containing 8-, 10-, and 12-nt ordered RNAs and two elongation complexes containing 14-nt RNAs. We suggest that promoter escape occurs in three major steps. First, the growing RNA displaces the B-reader element of the initiation factor TFIIB without evicting TFIIB. Second, the rewinding of the transcription bubble coincides with the eviction of TFIIA, TFIIB, and TBP. Third, the binding of DSIF and NELF facilitates TFIIE and TFIIH dissociation, establishing the paused elongation complex. This three-step model for promoter escape fills a gap in our understanding of the initiation-elongation transition of RNA Pol II transcription.
History
DepositionFeb 22, 2024-
Header (metadata) releaseApr 17, 2024-
Map releaseApr 17, 2024-
UpdateApr 24, 2024-
Current statusApr 24, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_19720.png

Downloads & links

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Map

FileDownload / File: emd_19720.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationComposite map for EC14b (sharpened)
Projections & slices

Image control

Size
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AxesX (Sec.)Y (Row.)Z (Col.)
1.05 Å/pix.
x 400 pix.
= 420. Å		1.05 Å/pix.
x 400 pix.
= 420. Å		1.05 Å/pix.
x 400 pix.
= 420. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.05 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 2.53
Minimum - Maximum-24.546524000000002 - 47.913820000000001
Average (Standard dev.)-0.000000000003973 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 419.99997 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_19720_msk_1.map
Projections & Slices
AxesZYX

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Additional map: Focused refined and locally filtered map for EC14b

Fileemd_19720_additional_1.map
AnnotationFocused refined and locally filtered map for EC14b
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Additional map: Half map corresponding to the map focused refined on Pol II

Fileemd_19720_additional_2.map
AnnotationHalf map corresponding to the map focused refined on Pol II
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AxesZYX

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Additional map: Half map corresponding to the map focused refined on Pol II

Fileemd_19720_additional_3.map
AnnotationHalf map corresponding to the map focused refined on Pol II
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Additional map: Mask for focused refined on Pol II

Fileemd_19720_additional_4.map
AnnotationMask for focused refined on Pol II
Projections & Slices
AxesZYX

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Half map: Half map corresponding to the map focused refined on EC14b

Fileemd_19720_half_map_1.map
AnnotationHalf map corresponding to the map focused refined on EC14b
Projections & Slices
AxesZYX

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Half map: Half map corresponding to the map focused refined on EC14b

Fileemd_19720_half_map_2.map
AnnotationHalf map corresponding to the map focused refined on EC14b
Projections & Slices
AxesZYX

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Sample components

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Entire : RNA polymerase II early elongation complex bound to TFIIE and TFI...

EntireName: RNA polymerase II early elongation complex bound to TFIIE and TFIIF - state b
Components
  • Complex: RNA polymerase II early elongation complex bound to TFIIE and TFIIF - state b
    • Complex: RNA polymerase II
      • Protein or peptide: DNA-directed RNA polymerase subunitPolymerase
      • Protein or peptide: DNA-directed RNA polymerase subunit betaPolymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB3Polymerase
      • Protein or peptide: RNA polymerase II subunit D
      • Protein or peptide: DNA-directed RNA polymerase II subunit EPolymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC2RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB7Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB9Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB11-aPolymerase
      • Protein or peptide: RNA polymerase II subunit K
    • Complex: DNA and RNA
      • DNA: Non-template DNA
      • RNA: RNA
      • DNA: Template DNA
    • Complex: Transcription factor IIE subunit 1 and Transcription factor IIF
      • Protein or peptide: General transcription factor IIF subunit 1
      • Protein or peptide: General transcription factor IIF subunit 2
      • Protein or peptide: General transcription factor IIE subunit 1
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: RNA polymerase II early elongation complex bound to TFIIE and TFI...

SupramoleculeName: RNA polymerase II early elongation complex bound to TFIIE and TFIIF - state b
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#18

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Supramolecule #2: RNA polymerase II

SupramoleculeName: RNA polymerase II / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#12
Source (natural)Organism: Sus scrofa (pig)

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Supramolecule #3: DNA and RNA

SupramoleculeName: DNA and RNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #13-#14, #17
Source (natural)Organism: unidentified adenovirus

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Supramolecule #4: Transcription factor IIE subunit 1 and Transcription factor IIF

SupramoleculeName: Transcription factor IIE subunit 1 and Transcription factor IIF
type: complex / ID: 4 / Parent: 1 / Macromolecule list: #15-#16, #18
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: DNA-directed RNA polymerase subunit

MacromoleculeName: DNA-directed RNA polymerase subunit / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 218.889547 KDa
SequenceString: MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIE LAKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE M DNKFGVEQ ...String:
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIE LAKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE M DNKFGVEQ PEGDEDLTKE KGHGGCGRYQ PRIRRSGLEL YAEWKHVNED SQEKKILLSP ERVHEIFKRI SDEECFVLGM EP RYARPEW MIVTVLPVPP LSVRPAVVMQ GSARNQDDLT HKLADIVKIN NQLRRNEQNG AAAHVIAEDV KLLQFHVATM VDN ELPGLP RAMQKSGRPL KSLKQRLKGK EGRVRGNLMG KRVDFSARTV ITPDPNLSID QVGVPRSIAA NMTFAEIVTP FNID RLQEL VRRGNSQYPG AKYIIRDNGD RIDLRFHPKP SDLHLQTGYK VERHMCDGDI VIFNRQPTLH KMSMMGHRVR ILPWS TFRL NLSVTTPYNA DFDGDEMNLH LPQSLETRAE IQELAMVPRM IVTPQSNRPV MGIVQDTLTA VRKFTKRDVF LERGEV MNL LMFLSTWDGK VPQPAILKPR PLWTGKQIFS LIIPGHINCI RTHSTHPDDE DSGPYKHISP GDTKVVVENG ELIMGIL CK KSLGTSAGSL VHISYLEMGH DITRLFYSNI QTVINNWLLI EGHTIGIGDS IADSKTYQDI QNTIKKAKQD VIEVIEKA H NNELEPTPGN TLRQTFENQV NRILNDARDK TGSSAQKSLS EYNNFKSMVV SGAKGSKINI SQVIAVVGQQ NVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQL RYGEDGLAGE SVEFQNLATL KPSNKAFEKK FRFDYTNERA LRRTLQEDLV KDVLSNAHIQ NELEREFERM R EDREVLRV IFPTGDSKVV LPCNLLRMIW NAQKIFHINP RLPSDLHPIK VVEGVKELSK KLVIVNGDDP LSRQAQENAT LL FNIHLRS TLCSRRMAEE FRLSGEAFDW LLGEIESKFN QAIAHPGEMV GALAAQSLGE PATQMTLNTF HYAGVSAKNV TLG VPRLKE LINISKKPKT PSLTVFLLGQ SARDAERAKD ILCRLEHTTL RKVTANTAIY YDPNPQSTVV AEDQEWVNVY YEMP DFDVA RISPWLLRVE LDRKHMTDRK LTMEQIAEKI NAGFGDDLNC IFNDDNAEKL VLRIRIMNSD ENKMQEEEEV VDKMD DDVF LRCIESNMLT DMTLQGIEQI SKVYMHLPQT DNKKKIIITE DGEFKALQEW ILETDGVSLM RVLSEKDVDP VRTTSN DIV EIFTVLGIEA VRKALERELY HVISFDGSYV NYRHLALLCD TMTCRGHLMA ITRHGVNRQD TGPLMKCSFE ETVDVLM EA AAHGESDPMK GVSENIMLGQ LAPAGTGCFD LLLDAEKCKY GMEIPTNIPG LGAAGPTGMF FGSAPSPMGG ISPAMTPW N QGATPAYGAW SPSVGSGMTP GAAGFSPSAA SDASGFSPGY SPAWSPTPGS PGSPGPSSPY IPSPGGAMSP SYSPTSPAY EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS P NYSPTSPN YTPTSPSYSP TSPSYSPTSP NYTPTSPNYS PTSPSYSPTS PSYSPTSPSY SPSSPRYTPQ SPTYTPSSPS YS PSSPSYS PTSPKYTPTS PSYSPSSPEY TPTSPKYSPT SPKYSPTSPK YSPTSPTYSP TTPKYSPTSP TYSPTSPVYT PTS PKYSPT SPTYSPTSPK YSPTSPTYSP TSPKGSTYSP TSPGYSPTSP TYSLTSPAIS PDDSDEEN

UniProtKB: DNA-directed RNA polymerase subunit

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Macromolecule #2: DNA-directed RNA polymerase subunit beta

MacromoleculeName: DNA-directed RNA polymerase subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 147.938594 KDa
SequenceString: MKPLRPENPP KAELKGLLFV QQHCKTRLHS VAVTRPRGAA TEESTPKLRM CSTNLSQALA YFRAGANLTA ASLWAGFRGS RRIFWERRK RKSLCLALRP GGACWRWLLA VSCVSLRGLG APGSCANMYD ADEDMQYDED DDEITPDLWQ EACWIVISSY F DEKGLVRQ ...String:
MKPLRPENPP KAELKGLLFV QQHCKTRLHS VAVTRPRGAA TEESTPKLRM CSTNLSQALA YFRAGANLTA ASLWAGFRGS RRIFWERRK RKSLCLALRP GGACWRWLLA VSCVSLRGLG APGSCANMYD ADEDMQYDED DDEITPDLWQ EACWIVISSY F DEKGLVRQ QLDSFDEFIQ MSVQRIVEDA PPIDLQAEAQ HASGEVEEPP RYLLKFEQIY LSKPTHWERD GAPSPMMPNE AR LRNLTYS APLYVDITKT VIKEGEEQLQ TQHQKTFIGK IPIMLRSTYC LLNGLTDRDL CELNECPLDP GGYFIINGSE KVL IAQEKM ATNTVYVFAK KDSKYAYTGE CRSCLENSSR PTSTIWVSML ARGGQGAKKS AIGQRIVATL PYIKQEVPII IVFR ALGFV SDRDILEHII YDFEDPEMME MVKPSLDEAF VIQEQNVALN FIGSRGAKPG VTKEKRIKYA KEVLQKEMLP HVGVS DFCE TKKAYFLGYM VHRLLLAALG RRELDDRDHY GNKRLDLAGP LLAFLFRGMF KNLLKEVRIY AQKFIDRGKD FNLELA IKT RIISDGLKYS LATGNWGDQK KAHQARAGVS QVLNRLTFAS TLSHLRRLNS PIGRDGKLAK PRQLHNTLWG MVCPAET PE GHAVGLVKNL ALMAYISVGS QPSPILEFLE EWSMENLEEI SPAAIADATK IFVNGCWVGI HKDPEQLMNT LRKLRRQM D IIVSEVSMIR DIREREIRIY TDAGRICRPL LIVEKQKLLL KKRHIDQLKE REYNNYSWQD LVASGVVEYI DTLEEETVM LAMTPDDLQE KEVAYCSTYT HCEIHPSMIL GVCASIIPFP DHNQSPRNTY QSAMGKQAMG VYITNFHVRM DTLAHVLYYP QKPLVTTRS MEYLRFRELP AGINSIVAIA SYTGYNQEDS VIMNRSAVDR GFFRSVFYRS YKEQESKKGF DQEEVFEKPT R ETCQGMRH AIYDKLDDDG LIAPGVRVSG DDVIIGKTVT LPENEDELEG TNRRYTKRDC STFLRTSETG IVDQVMVTLN QE GYKFCKI RVRSVRIPQI GDKFASRHGQ KGTCGIQYRQ EDMPFTCEGI TPDIIINPHA IPSRMTIGHL IECLQGKVSA NKG EIGDAT PFNDAVNVQK ISNLLSDYGY HLRGNEVLYN GFTGRKITSQ IFIGPTYYQR LKHMVDDKIH SRARGPIQIL NRQP MEGRS RDGGLRFGEM ERDCQIAHGA AQFLRERLFE ASDPYQVHVC NLCGIMAIAN TRTHTYECRG CRNKTQISLV RMPYA CKLL FQELMSMSIA PRMMSV

UniProtKB: DNA-directed RNA polymerase subunit beta

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Macromolecule #3: DNA-directed RNA polymerase II subunit RPB3

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 31.439074 KDa
SequenceString: MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH DEFIAHRLGL IPLTSDDIVD KLQYSRDCT CEEFCPECSV EFTLDVRCNE DQTRHVTSRD LISNSPRVIP VTSRNRDNDP SDYVEQDDIL IVKLRKGQEL R LRAYAKKG ...String:
MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH DEFIAHRLGL IPLTSDDIVD KLQYSRDCT CEEFCPECSV EFTLDVRCNE DQTRHVTSRD LISNSPRVIP VTSRNRDNDP SDYVEQDDIL IVKLRKGQEL R LRAYAKKG FGKEHAKWNP TAGVAFEYDP DNALRHTVYP KPEEWPKSEY SELDEDESQA PYDPNGKPER FYYNVESCGS LR PETIVLS ALSGLKKKLS DLQTQLSHEI QSDVLTIN

UniProtKB: DNA-directed RNA polymerase II subunit RPB3

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Macromolecule #4: RNA polymerase II subunit D

MacromoleculeName: RNA polymerase II subunit D / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 20.962621 KDa
SequenceString:
MWGPAQPYSD SALSPKPRPF RAVFRGSALP FPAVRVEVRG RSMAAGGSDP RAGDVEEDAS QLIFPKEFET AETLLNSEVH MLLEHRKQQ NESAEDEQEL SEVFMKTLNY TARFSRFKNR ETIASVRSLL LQKKLHKFEL ACLANLCPET AEESKALIPS L EGRFEDEE LQQILDDIQT KRSFQY

UniProtKB: RNA polymerase II subunit D

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Macromolecule #5: DNA-directed RNA polymerase II subunit E

MacromoleculeName: DNA-directed RNA polymerase II subunit E / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 24.644318 KDa
SequenceString: MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQFGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN ...String:
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQFGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN QLPRIQAGDP VARYFGIKRG QVVKIIRPSE TAGRYITYRL VQ

UniProtKB: DNA-directed RNA polymerase II subunit E

+
Macromolecule #6: DNA-directed RNA polymerases I, II, and III subunit RPABC2

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC2
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.477001 KDa
SequenceString:
MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY ERARVLGTRA LQIAMCAPVM VELEGETDP LLIAMKELKA RKIPIIIRRY LPDGSYEDWG VDELIISD

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC2

+
Macromolecule #7: DNA-directed RNA polymerase II subunit RPB7

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB7 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 19.314283 KDa
SequenceString:
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ PGRGFVLYPV KYKAIVFRPF KGEVVDAVV TQVNKVGLFT EIGPMSCFIS RHSIPSEMEF DPNSNPPCYK TMDEDIVIQQ DDEIRLKIVG TRVDKNDIFA I GSLMDDYL GLVS

UniProtKB: DNA-directed RNA polymerase subunit

+
Macromolecule #8: DNA-directed RNA polymerases I, II, and III subunit RPABC3

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC3
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 17.162273 KDa
SequenceString:
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI ASTLYEDGTL DDGEYNPTDD RPSRADQFE YVMYGKVYRI EGDETSTEAA TRLSAYVSYG GLLMRLQGDA NNLHGFEVDS RVYLLMKKLA F

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC3

+
Macromolecule #9: DNA-directed RNA polymerase II subunit RPB9

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB9 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.541221 KDa
SequenceString:
MEPDGTYEPG FVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH EVDELTQIIA DVSQDPTLPR TEDHPCQKC GHKEAVFFQS HSARAEDAMR LYYVCTAPHC GHRWTE

UniProtKB: DNA-directed RNA polymerase II subunit RPB9

+
Macromolecule #10: DNA-directed RNA polymerases I, II, and III subunit RPABC5

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC5
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.655123 KDa
SequenceString:
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL NYAPLEK

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC5

+
Macromolecule #11: DNA-directed RNA polymerase II subunit RPB11-a

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB11-a / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.310284 KDa
SequenceString:
MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG YKVPHPLEHK IIIRVQTTPD YSPQEAFTN AITDLISELS LLEERFRVAI KDKQEGIE

UniProtKB: DNA-directed RNA polymerase II subunit RPB11-a

+
Macromolecule #12: RNA polymerase II subunit K

MacromoleculeName: RNA polymerase II subunit K / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.018244 KDa
SequenceString:
MDTQKDVQPP KQQPMIYICG ECHTENEIKS RDPIRCRECG YRIMYKKRTK RLVVFDAR

UniProtKB: RNA polymerase II subunit K

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Macromolecule #15: General transcription factor IIF subunit 1

MacromoleculeName: General transcription factor IIF subunit 1 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 58.343578 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLK EFRPEDQPWL LRVNGKSGRK FKGIKKGGVT ENTSYYIFTQ CPDGAFEAFP VHNWYNFTPL ARHRTLTAEE A EEEWERRN ...String:
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLK EFRPEDQPWL LRVNGKSGRK FKGIKKGGVT ENTSYYIFTQ CPDGAFEAFP VHNWYNFTPL ARHRTLTAEE A EEEWERRN KVLNHFSIMQ QRRLKDQDQD EDEEEKEKRG RRKASELRIH DLEDDLEMSS DASDASGEEG GRVPKAKKKA PL AKGGRKK KKKKGSDDEA FEDSDDGDFE GQEVDYMSDG SSSSQEEPES KAKAPQQEEG PKGVDEQSDS SEESEEEKPP EED KEEEEE KKAPTPQEKK RRKDSSEESD SSEESDIDSE ASSALFMAKK KTPPKRERKP SGGSSRGNSR PGTPSAEGGS TSST LRAAA SKLEQGKRVS EMPAAKRLRL DTGPQSLSGK STPQPPSGKT TPNSGDVQVT EDAVRRYLTR KPMTTKDLLK KFQTK KTGL SSEQTVNVLA QILKRLNPER KMINDKMHFS LKE

UniProtKB: General transcription factor IIF subunit 1

+
Macromolecule #16: General transcription factor IIF subunit 2

MacromoleculeName: General transcription factor IIF subunit 2 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.427309 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVG GQTLTVFTES SSDKLSLEGI VVQRAECRPA ASENYMRLKR LQIEESSKPV RLSQQLDKVV TTNYKPVANH Q YNIEYERK ...String:
MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVG GQTLTVFTES SSDKLSLEGI VVQRAECRPA ASENYMRLKR LQIEESSKPV RLSQQLDKVV TTNYKPVANH Q YNIEYERK KKEDGKRARA DKQHVLDMLF SAFEKHQYYN LKDLVDITKQ PVVYLKEILK EIGVQNVKGI HKNTWELKPE YR HYQGEEK SD

UniProtKB: General transcription factor IIF subunit 2

+
Macromolecule #18: General transcription factor IIE subunit 1

MacromoleculeName: General transcription factor IIE subunit 1 / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 49.516094 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MADPDVLTEV PAALKRLAKY VIRGFYGIEH ALALDILIRN SCVKEEDMLE LLKFDRKQLR SVLNNLKGDK FIKCRMRVET AADGKTTRH NYYFINYRTL VNVVKYKLDH MRRRIETDER DSTNRASFKC PVCSSTFTDL EANQLFDPMT GTFRCTFCHT E VEEDESAM ...String:
MADPDVLTEV PAALKRLAKY VIRGFYGIEH ALALDILIRN SCVKEEDMLE LLKFDRKQLR SVLNNLKGDK FIKCRMRVET AADGKTTRH NYYFINYRTL VNVVKYKLDH MRRRIETDER DSTNRASFKC PVCSSTFTDL EANQLFDPMT GTFRCTFCHT E VEEDESAM PKKDARTLLA RFNEQIEPIY ALLRETEDVN LAYEILEPEP TEIPALKQSK DHAATTAGAA SLAGGHHREA WA TKGPSYE DLYTQNVVIN MDDQEDLHRA SLEGKSAKER PIWLRESTVQ GAYGSEDMKE GGIDMDAFQE REEGHAGPDD NEE VMRALL IHEKKTSSAM AGSVGAAAPV TAANGSDSES ETSESDDDSP PRPAAVAVHK REEDEEEDDE FEEVADDPIV MVAG RPFSY SEVSQRPELV AQMTPEEKEA YIAMGQRMFE DLFE

UniProtKB: General transcription factor IIE subunit 1

+
Macromolecule #13: Non-template DNA

MacromoleculeName: Non-template DNA / type: dna / ID: 13 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: unidentified adenovirus
Molecular weightTheoretical: 43.236555 KDa
SequenceString: (DG)(DT)(DG)(DT)(DT)(DC)(DC)(DT)(DG)(DA) (DA)(DG)(DG)(DG)(DG)(DG)(DG)(DC)(DT)(DA) (DT)(DA)(DA)(DA)(DA)(DG)(DG)(DG)(DG) (DG)(DT)(DG)(DG)(DG)(DG)(DG)(DC)(DG)(DC) (DG) (DT)(DT)(DC)(DG)(DT)(DC) ...String:
(DG)(DT)(DG)(DT)(DT)(DC)(DC)(DT)(DG)(DA) (DA)(DG)(DG)(DG)(DG)(DG)(DG)(DC)(DT)(DA) (DT)(DA)(DA)(DA)(DA)(DG)(DG)(DG)(DG) (DG)(DT)(DG)(DG)(DG)(DG)(DG)(DC)(DG)(DC) (DG) (DT)(DT)(DC)(DG)(DT)(DC)(DC)(DT) (DC)(DA)(DC)(DA)(DC)(DC)(DC)(DA)(DG)(DC) (DC)(DG) (DC)(DA)(DA)(DT)(DT)(DT)(DT) (DG)(DA)(DC)(DA)(DG)(DC)(DG)(DA)(DG)(DG) (DG)(DC)(DC) (DA)(DG)(DC)(DA)(DG)(DA) (DA)(DG)(DG)(DG)(DG)(DA)(DG)(DA)(DG)(DA) (DA)(DC)(DT)(DT) (DT)(DT)(DT)(DC)(DT) (DC)(DA)(DA)(DA)(DA)(DG)(DC)(DG)(DG)(DG) (DC)(DA)(DT)(DG)(DA) (DC)(DT)(DT)(DC) (DT)(DG)(DC)(DG)(DC)(DT)(DA)(DA)(DG)(DA) (DT)(DT)(DG)(DT)(DC)

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Macromolecule #17: Template DNA

MacromoleculeName: Template DNA / type: dna / ID: 17 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: unidentified adenovirus
Molecular weightTheoretical: 42.569098 KDa
SequenceString: (DG)(DA)(DC)(DA)(DA)(DT)(DC)(DT)(DT)(DA) (DG)(DC)(DG)(DC)(DA)(DG)(DA)(DA)(DG)(DT) (DC)(DA)(DT)(DG)(DC)(DC)(DC)(DG)(DC) (DT)(DT)(DT)(DT)(DG)(DA)(DG)(DA)(DA)(DA) (DA) (DA)(DG)(DT)(DT)(DC)(DT) ...String:
(DG)(DA)(DC)(DA)(DA)(DT)(DC)(DT)(DT)(DA) (DG)(DC)(DG)(DC)(DA)(DG)(DA)(DA)(DG)(DT) (DC)(DA)(DT)(DG)(DC)(DC)(DC)(DG)(DC) (DT)(DT)(DT)(DT)(DG)(DA)(DG)(DA)(DA)(DA) (DA) (DA)(DG)(DT)(DT)(DC)(DT)(DC)(DT) (DC)(DC)(DC)(DC)(DT)(DT)(DC)(DT)(DG)(DC) (DT)(DG) (DG)(DC)(DC)(DC)(DT)(DC)(DG) (DC)(DT)(DG)(DT)(DC)(DA)(DA)(DA)(DA)(DT) (DT)(DG)(DC) (DG)(DG)(DC)(DT)(DG)(DG) (DG)(DT)(DG)(DT)(DG)(DA)(DG)(DG)(DA)(DC) (DG)(DA)(DA)(DC) (DG)(DC)(DG)(DC)(DC) (DC)(DC)(DC)(DA)(DC)(DC)(DC)(DC)(DC)(DT) (DT)(DT)(DT)(DA)(DT) (DA)(DG)(DC)(DC) (DC)(DC)(DC)(DC)(DT)(DT)(DC)(DA)(DG)(DG) (DA)(DA)(DC)(DA)(DC)

+
Macromolecule #14: RNA

MacromoleculeName: RNA / type: rna / ID: 14 / Number of copies: 1
Source (natural)Organism: unidentified adenovirus
Molecular weightTheoretical: 4.427756 KDa
SequenceString:
ACACCCAGCC GCAA

+
Macromolecule #19: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 19 / Number of copies: 9 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #20: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 20 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.7000000000000001 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

12613

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF
Details: Different number of particles was used for different focused refined maps, as detailed in the manuscript.
Number images used: 50000

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