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- EMDB-30578: cryo-EM structure of human RNA polymerase III in apo state -

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Basic information

Entry
Database: EMDB / ID: EMD-30578
Titlecryo-EM structure of human RNA polymerase III in apo state
Map data
Sample
  • Complex: RNA Pol3 Apo
    • Protein or peptide: x 17 types
  • Ligand: x 2 types
KeywordsRNA Polymerase III / TRANSCRIPTION
Function / homology
Function and homology information


snRNA transcription by RNA polymerase III / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / calcitonin gene-related peptide receptor activity / DNA/RNA hybrid binding / regulation of transcription by RNA polymerase I / regulation of transcription by RNA polymerase III / RPAP3/R2TP/prefoldin-like complex / DNA polymerase III complex / Cytosolic sensors of pathogen-associated DNA ...snRNA transcription by RNA polymerase III / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / calcitonin gene-related peptide receptor activity / DNA/RNA hybrid binding / regulation of transcription by RNA polymerase I / regulation of transcription by RNA polymerase III / RPAP3/R2TP/prefoldin-like complex / DNA polymerase III complex / Cytosolic sensors of pathogen-associated DNA / 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 / RNA Polymerase III Abortive And Retractive Initiation / positive regulation of innate immune response / Abortive elongation of HIV-1 transcript in the absence of Tat / nucleobase-containing compound metabolic process / RNA Polymerase I Transcription Termination / FGFR2 alternative splicing / MicroRNA (miRNA) biogenesis / 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 / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / PIWI-interacting RNA (piRNA) biogenesis / 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 / termination of RNA polymerase III transcription / transcription initiation at RNA polymerase III promoter / RNA polymerase III activity / mRNA Splicing - Minor Pathway / RNA Polymerase I Transcription Initiation / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / transcription by RNA polymerase I / Processing of Capped Intron-Containing Pre-mRNA / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / transcription by RNA polymerase III / RNA polymerase II transcribes snRNA genes / neuropeptide signaling pathway / Tat-mediated elongation of the HIV-1 transcript / transcription elongation by RNA polymerase I / Formation of HIV-1 elongation complex containing HIV-1 Tat / tRNA transcription by RNA polymerase III / RNA polymerase I complex / RNA polymerase I activity / RNA polymerase III complex / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / Inhibition of DNA recombination at telomere / positive regulation of interferon-beta production / mRNA Splicing - Major Pathway / acrosomal vesicle / protein-DNA complex / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / ribonucleoside binding / fibrillar center / Activation of anterior HOX genes in hindbrain development during early embryogenesis / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / single-stranded DNA binding / 4 iron, 4 sulfur cluster binding / double-stranded DNA binding / defense response to virus / Estrogen-dependent gene expression / transcription by RNA polymerase II / cell population proliferation / nucleic acid binding / protein dimerization activity / protein stabilization / nuclear body / intracellular membrane-bounded organelle / innate immune response / nucleotide binding / centrosome / DNA-templated transcription / chromatin binding / magnesium ion binding / DNA binding / zinc ion binding
Similarity search - Function
DNA-directed RNA polymerase III subunit RPC5, C-terminal / DNA-directed RNA polymerase III subunit RPC5 C-terminal / DNA-directed RNA polymerase III subunit RPC4 / RNA polymerase III RPC4 / DNA-directed RNA polymerase III, subunit Rpc31 / DNA-directed RNA polymerase III subunit Rpc31 / Pol III subunit C11, C-terminal zinc ribbon / DNA-directed RNA polymerase III subunit Rpc5 / DNA-directed RNA polymerase III subunit RPC1, N-terminal / DNA-directed RNA polymerase III subunit RPC1, C-terminal ...DNA-directed RNA polymerase III subunit RPC5, C-terminal / DNA-directed RNA polymerase III subunit RPC5 C-terminal / DNA-directed RNA polymerase III subunit RPC4 / RNA polymerase III RPC4 / DNA-directed RNA polymerase III, subunit Rpc31 / DNA-directed RNA polymerase III subunit Rpc31 / Pol III subunit C11, C-terminal zinc ribbon / DNA-directed RNA polymerase III subunit Rpc5 / DNA-directed RNA polymerase III subunit RPC1, N-terminal / DNA-directed RNA polymerase III subunit RPC1, C-terminal / RPC5 protein / RNA polymerase III, subunit Rpc25 / DNA-directed RNA polymerase III subunit RPC9 / RNA polymerase III subunit Rpc25 / RNA polymerase Rpc34 / RNA polymerase III Rpc82, C -terminal / RNA polymerase Rpc34-like / DNA-directed RNA polymerase III subunit RPC3 / RNA polymerase Rpc34 subunit / RNA polymerase III subunit RPC82 / DNA-directed RNA polymerase III subunit RPC3, helical hairpin domain / POLR3C, C-terminal winged-helix domain / RNA polymerase III subunit RPC82-related, helix-turn-helix / RNA polymerase III subunit RPC82 helix-turn-helix domain / DNA-directed RNA polymerase, subunit E/RPC8 / DNA-directed RNA polymerases I and III subunit AC19 / DNA-directed RNA polymerases I and III subunit AC40 / RNA polymerase Rpb4/RPC9, core / DNA-directed RNA-polymerase II subunit / Rpb4/RPC9 superfamily / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Zinc finger TFIIS-type signature. / HRDC-like superfamily / RNA polymerase Rpb7-like , N-terminal / RNA polymerase Rpb7-like, N-terminal domain superfamily / RNA polymerase subunit Rpb7-like / SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / DNA-directed RNA polymerase, M/15kDa subunit / RNA polymerases M/15 Kd subunit / RNA polymerase subunit 9 / 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 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, subunit RPB6 / 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, 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 Rpb11, 13-16kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo11 / RNA polymerases L / 13 to 16 Kd subunits signature. / Zinc finger, TFIIS-type / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / RNA polymerase subunit RPABC4/transcription elongation factor Spt4 / DNA-directed RNA polymerase, RBP11-like dimerisation domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerase, subunit H/Rpb5 C-terminal / 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. / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RPB6/omega subunit-like superfamily / RNA polymerase Rpb1, clamp domain superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type
Similarity search - Domain/homology
DNA-directed RNA polymerase III subunit RPC1 / DNA-directed RNA polymerases I and III subunit RPAC1 / DNA-directed RNA polymerase III subunit RPC7 / DNA-directed RNA polymerase III subunit RPC9 / DNA-directed RNA polymerase III subunit RPC4 / DNA-directed RNA polymerases I and III subunit RPAC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 ...DNA-directed RNA polymerase III subunit RPC1 / DNA-directed RNA polymerases I and III subunit RPAC1 / DNA-directed RNA polymerase III subunit RPC7 / DNA-directed RNA polymerase III subunit RPC9 / DNA-directed RNA polymerase III subunit RPC4 / DNA-directed RNA polymerases I and III subunit RPAC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase III subunit RPC3 / DNA-directed RNA polymerase III subunit RPC6 / DNA-directed RNA polymerase III subunit RPC5 / DNA-directed RNA polymerase III subunit RPC2 / DNA-directed RNA polymerase III subunit RPC10 / DNA-directed RNA polymerase III subunit RPC8
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsWang Q / Wan F
CitationJournal: Nat Struct Mol Biol / Year: 2021
Title: Structural insights into transcriptional regulation of human RNA polymerase III.
Authors: Qianmin Wang / Shaobai Li / Futang Wan / Youwei Xu / Zhenfang Wu / Mi Cao / Pengfei Lan / Ming Lei / Jian Wu /
Abstract: RNA polymerase III (Pol III) synthesizes structured, essential small RNAs, such as transfer RNA, 5S ribosomal RNA and U6 small nuclear RNA. Pol III, the largest nuclear RNA polymerase, is composed of ...RNA polymerase III (Pol III) synthesizes structured, essential small RNAs, such as transfer RNA, 5S ribosomal RNA and U6 small nuclear RNA. Pol III, the largest nuclear RNA polymerase, is composed of a conserved core region and eight constitutive regulatory subunits, but how these factors jointly regulate Pol III transcription remains unclear. Here, we present cryo-EM structures of human Pol III in both apo and elongating states, which unveil both an orchestrated movement during the apo-to-elongating transition and an unexpected apo state in which the RPC7 subunit tail occupies the DNA-RNA-binding cleft of Pol III, suggesting that RPC7 plays important roles in both autoinhibition and transcription initiation. The structures also reveal a proofreading mechanism for the TFIIS-like subunit RPC10, which stably retains its catalytic position in the secondary channel, explaining the high fidelity of Pol III transcription. Our work provides an integrated picture of the mechanism of Pol III transcription regulation.
History
DepositionSep 25, 2020-
Header (metadata) releaseFeb 17, 2021-
Map releaseFeb 17, 2021-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.007
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.007
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7d59
  • Surface level: 0.007
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_30578.png

Downloads & links

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Map

FileDownload / File: emd_30578.map.gz / Format: CCP4 / Size: 144.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 336 pix.
= 366.24 Å		1.09 Å/pix.
x 336 pix.
= 366.24 Å		1.09 Å/pix.
x 336 pix.
= 366.24 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.09 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.007 / Movie #1: 0.007
Minimum - Maximum-0.020658182 - 0.056506447
Average (Standard dev.)0.0000009774645 (±0.0014684692)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions336336336
Spacing336336336
CellA=B=C: 366.24002 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.091.091.09
M x/y/z336336336
origin x/y/z0.0000.0000.000
length x/y/z366.240366.240366.240
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS336336336
D min/max/mean-0.0210.0570.000

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Supplemental data

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Sample components

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Entire : RNA Pol3 Apo

EntireName: RNA Pol3 Apo
Components
  • Complex: RNA Pol3 Apo
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC1
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC2
    • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC1
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC9
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC1
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC2
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC8
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC10
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5
    • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC2
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC4
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC5
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC4
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC3
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC6
    • Protein or peptide: DNA-directed RNA polymerase III subunit RPC7
  • Ligand: ZINC ION
  • Ligand: IRON/SULFUR CLUSTER

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Supramolecule #1: RNA Pol3 Apo

SupramoleculeName: RNA Pol3 Apo / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#17
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: DNA-directed RNA polymerase III subunit RPC1

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 155.860125 KDa
SequenceString: MVKEQFRETD VAKKISHICF GMKSPEEMRQ QAHIQVVSKN LYSQDNQHAP LLYGVLDHRM GTSEKDRPCE TCGKNLADCL GHYGYIDLE LPCFHVGYFR AVIGILQMIC KTCCHIMLSQ EEKKQFLDYL KRPGLTYLQK RGLKKKISDK CRKKNICHHC G AFNGTVKK ...String:
MVKEQFRETD VAKKISHICF GMKSPEEMRQ QAHIQVVSKN LYSQDNQHAP LLYGVLDHRM GTSEKDRPCE TCGKNLADCL GHYGYIDLE LPCFHVGYFR AVIGILQMIC KTCCHIMLSQ EEKKQFLDYL KRPGLTYLQK RGLKKKISDK CRKKNICHHC G AFNGTVKK CGLLKIIHEK YKTNKKVVDP IVSNFLQSFE TAIEHNKEVE PLLGRAQENL NPLVVLNLFK RIPAEDVPLL LM NPEAGKP SDLILTRLLV PPLCIRPSVV SDLKSGTNED DLTMKLTEII FLNDVIKKHR ISGAKTQMIM EDWDFLQLQC ALY INSELS GIPLNMAPKK WTRGFVQRLK GKQGRFRGNL SGKRVDFSGR TVISPDPNLR IDEVAVPVHV AKILTFPEKV NKAN INFLR KLVQNGPEVH PGANFIQQRH TQMKRFLKYG NREKMAQELK YGDIVERHLI DGDVVLFNRQ PSLHKLSIMA HLARV KPHR TFRFNECVCT PYNADFDGDE MNLHLPQTEE AKAEALVLMG TKANLVTPRN GEPLIAAIQD FLTGAYLLTL KDTFFD RAK ACQIIASILV GKDEKIKVRL PPPTILKPVT LWTGKQIFSV ILRPSDDNPV RANLRTKGKQ YCGKGEDLCA NDSYVTI QN SELMSGSMDK GTLGSGSKNN IFYILLRDWG QNEAADAMSR LARLAPVYLS NRGFSIGIGD VTPGQGLLKA KYELLNAG Y KKCDEYIEAL NTGKLQQQPG CTAEETLEAL ILKELSVIRD HAGSACLREL DKSNSPLTMA LCGSKGSFIN ISQMIACVG QQAISGSRVP DGFENRSLPH FEKHSKLPAA KGFVANSFYS GLTPTEFFFH TMAGREGLVD TAVKTAETGY MQRRLVKSLE DLCSQYDLT VRSSTGDIIQ FIYGGDGLDP AAMEGKDEPL EFKRVLDNIK AVFPCPSEPA LSKNELILTT ESIMKKSEFL C CQDSFLQE IKKFIKGVSE KIKKTRDKYG INDNGTTEPR VLYQLDRITP TQVEKFLETC RDKYMRAQME PGSAVGALCA QS IGEPGTQ MTLKTFHFAG VASMNITLGV PRIKEIINAS KAISTPIITA QLDKDDDADY ARLVKGRIEK TLLGEISEYI EEV FLPDDC FILVKLSLER IRLLRLEVNA ETVRYSICTS KLRVKPGDVA VHGEAVVCVT PRENSKSSMY YVLQFLKEDL PKVV VQGIP EVSRAVIHID EQSGKEKYKL LVEGDNLRAV MATHGVKGTR TTSNNTYEVE KTLGIEAART TIINEIQYTM VNHGM SIDR RHVMLLSDLM TYKGEVLGIT RFGLAKMKES VLMLASFEKT ADHLFDAAYF GQKDSVCGVS ECIIMGIPMN IGTGLF KLL HKADRDPNPP KRPLIFDTNE FHIPLVT

UniProtKB: DNA-directed RNA polymerase III subunit RPC1

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Macromolecule #2: DNA-directed RNA polymerase III subunit RPC2

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 127.953891 KDa
SequenceString: MDVLAEEFGN LTPEQLAAPI PTVEEKWRLL PAFLKVKGLV KQHIDSFNYF INVEIKKIMK ANEKVTSDAD PMWYLKYLNI YVGLPDVEE SFNVTRPVSP HECRLRDMTY SAPITVDIEY TRGSQRIIRN ALPIGRMPIM LRSSNCVLTG KTPAEFAKLN E CPLDPGGY ...String:
MDVLAEEFGN LTPEQLAAPI PTVEEKWRLL PAFLKVKGLV KQHIDSFNYF INVEIKKIMK ANEKVTSDAD PMWYLKYLNI YVGLPDVEE SFNVTRPVSP HECRLRDMTY SAPITVDIEY TRGSQRIIRN ALPIGRMPIM LRSSNCVLTG KTPAEFAKLN E CPLDPGGY FIVKGVEKVI LIQEQLSKNR IIVEADRKGA VGASVTSSTH EKKSRTNMAV KQGRFYLRHN TLSEDIPIVI IF KAMGVES DQEIVQMIGT EEHVMAAFGP SLEECQKAQI FTQMQALKYI GNKVRRQRMW GGGPKKTKIE EARELLASTI LTH VPVKEF NFRAKCIYTA VMVRRVILAQ GDNKVDDRDY YGNKRLELAG QLLSLLFEDL FKKFNSEMKK IADQVIPKQR AAQF DVVKH MRQDQITNGM VNAISTGNWS LKRFKMDRQG VTQVLSRLSY ISALGMMTRI SSQFEKTRKV SGPRSLQPSQ WGMLC PSDT PEGEACGLVK NLALMTHITT DMEDGPIVKL ASNLGVEDVN LLCGEELSYP NVFLVFLNGN ILGVIRDHKK LVNTFR LMR RAGYINEFVS ISTNLTDRCV YISSDGGRLC RPYIIVKKQK PAVTNKHMEE LAQGYRNFED FLHESLVEYL DVNEEND CN IALYEHTINK DTTHLEIEPF TLLGVCAGLI PYPHHNQSPR NTYQCAMGKQ AMGTIGYNQR NRIDTLMYLL AYPQKPMV K TKTIELIEFE KLPAGQNATV AVMSYSGYDI EDALVLNKAS LDRGFGRCLV YKNAKCTLKR YTNQTFDKVM GPMLDAATR KPIWRHEILD ADGICSPGEK VENKQVLVNK SMPTVTQIPL EGSNVPQQPQ YKDVPITYKG ATDSYIEKVM ISSNAEDAFL IKMLLRQTR RPEIGDKFSS RHGQKGVCGL IVPQEDMPFC DSGICPDIIM NPHGFPSRMT VGKLIELLAG KAGVLDGRFH Y GTAFGGSK VKDVCEDLVR HGYNYLGKDY VTSGITGEPL EAYIYFGPVY YQKLKHMVLD KMHARARGPR AVLTRQPTEG RS RDGGLRL GEMERDCLIG YGASMLLLER LMISSDAFEV DVCGQCGLLG YSGWCHYCKS SCHVSSLRIP YACKLLFQEL QSM NIIPRL KLSKYNE

UniProtKB: DNA-directed RNA polymerase III subunit RPC2

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Macromolecule #3: DNA-directed RNA polymerases I and III subunit RPAC1

MacromoleculeName: DNA-directed RNA polymerases I and III subunit RPAC1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.301672 KDa
SequenceString: MAASQAVEEM RSRVVLGEFG VRNVHTTDFP GNYSGYDDAW DQDRFEKNFR VDVVHMDENS LEFDMVGIDA AIANAFRRIL LAEVPTMAV EKVLVYNNTS IVQDEILAHR LGLIPIHADP RLFEYRNQGD EEGTEIDTLQ FRLQVRCTRN PHAAKDSSDP N ELYVNHKV ...String:
MAASQAVEEM RSRVVLGEFG VRNVHTTDFP GNYSGYDDAW DQDRFEKNFR VDVVHMDENS LEFDMVGIDA AIANAFRRIL LAEVPTMAV EKVLVYNNTS IVQDEILAHR LGLIPIHADP RLFEYRNQGD EEGTEIDTLQ FRLQVRCTRN PHAAKDSSDP N ELYVNHKV YTRHMTWIPL GNQADLFPEG TIRPVHDDIL IAQLRPGQEI DLLMHCVKGI GKDHAKFSPV ATASYRLLPD IT LLEPVEG EAAEELSRCF SPGVIEVQEV QGKKVARVAN PRLDTFSREI FRNEKLKKVV RLARVRDHYI FSVESTGVLP PDV LVSEAI KVLMGKCRRF LDELDAVQMD

UniProtKB: DNA-directed RNA polymerases I and III subunit RPAC1

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Macromolecule #4: DNA-directed RNA polymerase III subunit RPC9

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC9 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.89399 KDa
SequenceString:
MEVKDANSAL LSNYEVFQLL TDLKEQRKES GKNKHSSGQQ NLNTITYETL KYISKTPCRH QSPEIVREFL TALKSHKLTK AEKLQLLNH RPVTAVEIQL MVEESEERLT EEQIEALLHT VTSILPAEPE AEQKKNTNSN VAMDEEDPA

UniProtKB: DNA-directed RNA polymerase III subunit RPC9

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Macromolecule #5: DNA-directed RNA polymerases I, II, and III subunit RPABC1

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC1
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.584223 KDa
SequenceString: MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN ...String:
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN QLPRIQAGDP VARYFGIKRG QVVKIIRPSE TAGRYITYRL VQ

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC1

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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: Homo sapiens (human)
Molecular weightTheoretical: 14.491026 KDa
SequenceString:
MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY ERARVLGTRA LQIAMCAPVM VELEGETDP LLIAMKELKA RKIPIIIRRY LPDGSYEDWG VDELIITD

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

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Macromolecule #7: DNA-directed RNA polymerase III subunit RPC8

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC8 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.938846 KDa
SequenceString: MFVLVEMVDT VRIPPWQFER KLNDSIAEEL NKKLANKVVY NVGLCICLFD ITKLEDAYVF PGDGASHTKV HFRCVVFHPF LDEILIGKI KGCSPEGVHV SLGFFDDILI PPESLQQPAK FDEAEQVWVW EYETEEGAHD LYMDTGEEIR FRVVDESFVD T SPTGPSSA ...String:
MFVLVEMVDT VRIPPWQFER KLNDSIAEEL NKKLANKVVY NVGLCICLFD ITKLEDAYVF PGDGASHTKV HFRCVVFHPF LDEILIGKI KGCSPEGVHV SLGFFDDILI PPESLQQPAK FDEAEQVWVW EYETEEGAHD LYMDTGEEIR FRVVDESFVD T SPTGPSSA DATTSSEELP KKEAPYTLVG SISEPGLGLL SWWTSN

UniProtKB: DNA-directed RNA polymerase III subunit RPC8

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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: Homo sapiens (human)
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

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Macromolecule #9: DNA-directed RNA polymerase III subunit RPC10

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC10 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.354104 KDa
SequenceString:
MLLFCPGCGN GLIVEEGQRC HRFSCNTCPY VHNITRKVTN RKYPKLKEVD DVLGGAAAWE NVDSTAESCP KCEHPRAYFM QLQTRSADE PMTTFYKCCN AQCGHRWRD

UniProtKB: DNA-directed RNA polymerase III subunit RPC10

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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: Homo sapiens (human)
Molecular weightTheoretical: 7.655123 KDa
SequenceString:
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL NYAPLEK

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Macromolecule #11: DNA-directed RNA polymerases I and III subunit RPAC2

MacromoleculeName: DNA-directed RNA polymerases I and III subunit RPAC2 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.259222 KDa
SequenceString:
MEEDQELERK ISGLKTSMAE GERKTALEMV QAAGTDRHCV TFVLHEEDHT LGNSLRYMIM KNPEVEFCGY TTTHPSESKI NLRIQTRGT LPAVEPFQRG LNELMNVCQH VLDKFEASIK DYKDQKASRN ESTF

UniProtKB: DNA-directed RNA polymerases I and III subunit RPAC2

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Macromolecule #12: DNA-directed RNA polymerases I, II, and III subunit RPABC4

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC4
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.018244 KDa
SequenceString:
MDTQKDVQPP KQQPMIYICG ECHTENEIKS RDPIRCRECG YRIMYKKRTK RLVVFDAR

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC4

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Macromolecule #13: DNA-directed RNA polymerase III subunit RPC5

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC5 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 80.004031 KDa
SequenceString: MANEEDDPVV QEIDVYLAKS LAEKLYLFQY PVRPASMTYD DIPHLSAKIK PKQQKVELEM AIDTLNPNYC RSKGEQIALN VDGACADET STYSSKLMDK QTFCSSQTTS NTSRYAAALY RQGELHLTPL HGILQLRPSF SYLDKADAKH REREAANEAG D SSQDEAED ...String:
MANEEDDPVV QEIDVYLAKS LAEKLYLFQY PVRPASMTYD DIPHLSAKIK PKQQKVELEM AIDTLNPNYC RSKGEQIALN VDGACADET STYSSKLMDK QTFCSSQTTS NTSRYAAALY RQGELHLTPL HGILQLRPSF SYLDKADAKH REREAANEAG D SSQDEAED DVKQITVRFS RPESEQARQR RVQSYEFLQK KHAEEPWVHL HYYGLRDSRS EHERQYLLCP GSSGVENTEL VK SPSEYLM MLMPPSQEEE KDKPVAPSNV LSMAQLRTLP LADQIKILMK NVKVMPFANL MSLLGPSIDS VAVLRGIQKV AML VQGNWV VKSDILYPKD SSSPHSGVPA EVLCRGRDFV MWKFTQSRWV VRKEVATVTK LCAEDVKDFL EHMAVVRINK GWEF ILPYD GEFIKKHPDV VQRQHMLWTG IQAKLEKVYN LVKETMPKKP DAQSGPAGLV CGDQRIQVAK TKAQQNHALL ERELQ RRKE QLRVPAVPPG VRIKEEPVSE EGEEDEEQEA EEEPMDTSPS GLHSKLANGL PLGRAAGTDS FNGHPPQGCA STPVAR ELK AFVEATFQRQ FVLTLSELKR LFNLHLASLP PGHTLFSGIS DRMLQDTVLA AGCKQILVPF PPQTAASPDE QKVFALW ES GDMSDQHRQV LLEIFSKNYR VRRNMIQSRL TQECGEDLSK QEVDKVLKDC CVSYGGMWYL KGTVQS

UniProtKB: DNA-directed RNA polymerase III subunit RPC5

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Macromolecule #14: DNA-directed RNA polymerase III subunit RPC4

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC4 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.471875 KDa
SequenceString: MSEGNAAGEP STPGGPRPLL TGARGLIGRR PAPPLTPGRL PSIRSRDLTL GGVKKKTFTP NIISRKIKEE PKEEVTVKKE KRERDRDRQ REGHGRGRGR PEVIQSHSIF EQGPAEMMKK KGNWDKTVDV SDMGPSHIIN IKKEKRETDE ETKQILRMLE K DDFLDDPG ...String:
MSEGNAAGEP STPGGPRPLL TGARGLIGRR PAPPLTPGRL PSIRSRDLTL GGVKKKTFTP NIISRKIKEE PKEEVTVKKE KRERDRDRQ REGHGRGRGR PEVIQSHSIF EQGPAEMMKK KGNWDKTVDV SDMGPSHIIN IKKEKRETDE ETKQILRMLE K DDFLDDPG LRNDTRNMPV QLPLAHSGWL FKEENDEPDV KPWLAGPKEE DMEVDIPAVK VKEEPRDEEE EAKMKAPPKA AR KTPGLPK DVSVAELLRE LSLTKEEELL FLQLPDTLPG QPPTQDIKPI KTEVQGEDGQ VVLIKQEKDR EAKLAENACT LAD LTEGQV GKLLIRKSGR VQLLLGKVTL DVTMGTACSF LQELVSVGLG DSRTGEMTVL GHVKHKLVCS PDFESLLDHK HR

UniProtKB: DNA-directed RNA polymerase III subunit RPC4

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Macromolecule #15: DNA-directed RNA polymerase III subunit RPC3

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC3 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 60.692555 KDa
SequenceString: MTQAEIKLCS LLLQEHFGEI VEKIGVHLIR TGSQPLRVIA HDTGTSLDQV KKALCVLVQH NLVSYQVHKR GVVEYEAQCS RVLRMLRYP RYIYTTKTLY SDTGELIVEE LLLNGKLTMS AVVKKVADRL TETMEDGKTM DYAEVSNTFV RLADTHFVQR C PSVPTTEN ...String:
MTQAEIKLCS LLLQEHFGEI VEKIGVHLIR TGSQPLRVIA HDTGTSLDQV KKALCVLVQH NLVSYQVHKR GVVEYEAQCS RVLRMLRYP RYIYTTKTLY SDTGELIVEE LLLNGKLTMS AVVKKVADRL TETMEDGKTM DYAEVSNTFV RLADTHFVQR C PSVPTTEN SDPGPPPPAP TLVINEKDMY LVPKLSLIGK GKRRRSSDED AAGEPKAKRP KYTTDNKEPI PDDGIYWQAN LD RFHQHFR DQAIVSAVAN RMDQTSSEIV RTMLRMSEIT TSSSAPFTQP LSSNEIFRSL PVGYNISKQV LDQYLTLLAD DPL EFVGKS GDSGGGMYVI NLHKALASLA TATLESVVQE RFGSRCARIF RLVLQKKHIE QKQVEDFAMI PAKEAKDMLY KMLS ENFMS LQEIPKTPDH APSRTFYLYT VNILSAARML LHRCYKSIAN LIERRQFETK ENKRLLEKSQ RVEAIIASMQ ATGAE EAQL QEIEEMITAP ERQQLETLKR NVNKLDASEI QVDETIFLLE SYIECTMKRQ

UniProtKB: DNA-directed RNA polymerase III subunit RPC3

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Macromolecule #16: DNA-directed RNA polymerase III subunit RPC6

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC6 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 35.726914 KDa
SequenceString: MAEVKVKVQP PDADPVEIEN RIIELCHQFP HGITDQVIQN EMPHIEAQQR AVAINRLLSM GQLDLLRSNT GLLYRIKDSQ NAGKMKGSD NQEKLVYQII EDAGNKGIWS RDIRYKSNLP LTEINKILKN LESKKLIKAV KSVAASKKKV YMLYNLQPDR S VTGGAWYS ...String:
MAEVKVKVQP PDADPVEIEN RIIELCHQFP HGITDQVIQN EMPHIEAQQR AVAINRLLSM GQLDLLRSNT GLLYRIKDSQ NAGKMKGSD NQEKLVYQII EDAGNKGIWS RDIRYKSNLP LTEINKILKN LESKKLIKAV KSVAASKKKV YMLYNLQPDR S VTGGAWYS DQDFESEFVE VLNQQCFKFL QSKAETARES KQNPMIQRNS SFASSHEVWK YICELGISKV ELSMEDIETI LN TLIYDGK VEMTIIAAKE GTVGSVDGHM KLYRAVNPII PPTGLVRAPC GLCPVFDDCH EGGEISPSNC IYMTEWLEF

UniProtKB: DNA-directed RNA polymerase III subunit RPC6

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Macromolecule #17: DNA-directed RNA polymerase III subunit RPC7

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC7 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.95351 KDa
SequenceString: MAGNKGRGRA AYTFNIEAVG FSKGEKLPDV VLKPPPLFPD TDYKPVPLKT GEGEEYMLAL KQELRETMKR MPYFIETPEE RQDIERYSK RYMKVYKEEW IPDWRRLPRE MMPRNKCKKA GPKPKKAKDA GKGTPLTNTE DVLKKMEELE KRGDGEKSDE E NEEKEGSK ...String:
MAGNKGRGRA AYTFNIEAVG FSKGEKLPDV VLKPPPLFPD TDYKPVPLKT GEGEEYMLAL KQELRETMKR MPYFIETPEE RQDIERYSK RYMKVYKEEW IPDWRRLPRE MMPRNKCKKA GPKPKKAKDA GKGTPLTNTE DVLKKMEELE KRGDGEKSDE E NEEKEGSK EKSKEGDDDD DDDAAEQEEY DEEEQEEEND YINSYFEDGD DFGADSDDNM DEATY

UniProtKB: DNA-directed RNA polymerase III subunit RPC7

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Macromolecule #18: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 18 / Number of copies: 7 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #19: IRON/SULFUR CLUSTER

MacromoleculeName: IRON/SULFUR CLUSTER / type: ligand / ID: 19 / Number of copies: 1 / Formula: SF4
Molecular weightTheoretical: 351.64 Da
Chemical component information

ChemComp-FS1:
IRON/SULFUR CLUSTER

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 264514
Initial angle assignmentType: COMMON LINE
Final angle assignmentType: MAXIMUM LIKELIHOOD

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