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- EMDB-0241: Yeast apo RNA polymerase I* -

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Basic information

Entry
Database: EMDB / ID: EMD-0241
TitleYeast apo RNA polymerase I*
Map dataYeast apo RNA polymerase I*
Sample
  • Complex: Yeast apo RNA polymerase I*
    • Protein or peptide: x 12 types
  • Ligand: x 1 types
Keywordstranscription / polymerase / nucleotide / elongation
Function / homology
Function and homology information


RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening ...RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / TP53 Regulates Transcription of DNA Repair Genes / 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 / RNA Polymerase II Pre-transcription Events / RNA-templated transcription / Formation of TC-NER Pre-Incision Complex / regulation of cell size / transcription initiation at RNA polymerase III promoter / RNA Polymerase I Promoter Escape / termination of RNA polymerase I transcription / nucleolar large rRNA transcription by RNA polymerase I / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription initiation at RNA polymerase I promoter / Estrogen-dependent gene expression / transcription by RNA polymerase III / Dual incision in TC-NER / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / promoter-specific chromatin binding / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / peroxisome / ribosome biogenesis / nucleic acid binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / protein dimerization activity / nucleolus / negative regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm
Similarity search - Function
RNA polymerase I, subunit Rpa14, fungi / Yeast RNA polymerase I subunit RPA14 / Rpa43, N-terminal ribonucleoprotein (RNP) domain / Pol I subunit A12, C-terminal zinc ribbon / RPA43, OB domain / RPA43 OB domain in RNA Pol I / DNA-directed RNA polymerase I subunit RPA2, domain 4 / DNA-directed RNA pol I, largest subunit / : / RNA polymerase I, Rpa2 specific domain ...RNA polymerase I, subunit Rpa14, fungi / Yeast RNA polymerase I subunit RPA14 / Rpa43, N-terminal ribonucleoprotein (RNP) domain / Pol I subunit A12, C-terminal zinc ribbon / RPA43, OB domain / RPA43 OB domain in RNA Pol I / DNA-directed RNA polymerase I subunit RPA2, domain 4 / DNA-directed RNA pol I, largest subunit / : / RNA polymerase I, Rpa2 specific domain / DNA-directed RNA polymerases I and III subunit AC19 / DNA-directed RNA polymerases I and III subunit AC40 / Zinc finger TFIIS-type signature. / 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 / 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 RPB6 / 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, 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. / RNA polymerase subunit RPABC4/transcription elongation factor Spt4 / Zinc finger, TFIIS-type / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / DNA-directed RNA polymerase, RBP11-like dimerisation domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerase, subunit H/Rpb5 C-terminal / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / 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. / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / RNA polymerase Rpb1, clamp domain superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, N-terminal / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase Rpb2, domain 2 / RNA polymerase I subunit A N-terminus / RNA polymerase, RBP11-like subunit / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3
Similarity search - Domain/homology
DNA-directed RNA polymerases I and III subunit RPAC1 / DNA-directed RNA polymerase I subunit RPA190 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase I subunit RPA135 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerases I and III subunit RPAC2 / DNA-directed RNA polymerase I subunit RPA12 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 ...DNA-directed RNA polymerases I and III subunit RPAC1 / DNA-directed RNA polymerase I subunit RPA190 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase I subunit RPA135 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerases I and III subunit RPAC2 / DNA-directed RNA polymerase I subunit RPA12 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / DNA-directed RNA polymerase I subunit RPA43 / DNA-directed RNA polymerase I subunit RPA14
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.21 Å
AuthorsTafur L / Sadian Y
Funding support Germany, 1 items
OrganizationGrant numberCountry
European Research CouncilERC-2013-AdG340964-POL1PIC Germany
CitationJournal: Elife / Year: 2019
Title: The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34.5 heterodimer and rearrangement of subunit A12.2.
Authors: Lucas Tafur / Yashar Sadian / Jonas Hanske / Rene Wetzel / Felix Weis / Christoph W Müller /
Abstract: RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-electron microscopy (EM) structures of Pol I initiation and elongation complexes have given first ...RNA polymerase (Pol) I is a 14-subunit enzyme that solely transcribes pre-ribosomal RNA. Cryo-electron microscopy (EM) structures of Pol I initiation and elongation complexes have given first insights into the molecular mechanisms of Pol I transcription. Here, we present cryo-EM structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution that provide additional insight into the functional interplay between the Pol I-specific transcription-like factors A49-A34.5 and A12.2. Strikingly, most of the nucleotide-bound ECs lack the A49-A34.5 heterodimer and adopt a Pol II-like conformation, in which the A12.2 C-terminal domain is bound in a previously unobserved position at the A135 surface. Our structural and biochemical data suggest a mechanism where reversible binding of the A49-A34.5 heterodimer could contribute to the regulation of Pol I transcription initiation and elongation.
History
DepositionSep 11, 2018-
Header (metadata) releaseOct 24, 2018-
Map releaseApr 3, 2019-
UpdateMay 15, 2024-
Current statusMay 15, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0777
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.0777
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6hls
  • Surface level: 0.0777
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0241.png

Downloads & links

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Map

FileDownload / File: emd_0241.map.gz / Format: CCP4 / Size: 67 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationYeast apo RNA polymerase I*
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.04 Å/pix.
x 260 pix.
= 270.4 Å		1.04 Å/pix.
x 260 pix.
= 270.4 Å		1.04 Å/pix.
x 260 pix.
= 270.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.04 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0777 / Movie #1: 0.0777
Minimum - Maximum-0.19483472 - 0.3158225
Average (Standard dev.)-0.00028422332 (±0.016766652)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions260260260
Spacing260260260
CellA=B=C: 270.4 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.041.041.04
M x/y/z260260260
origin x/y/z0.0000.0000.000
length x/y/z270.400270.400270.400
α/β/γ90.00090.00090.000
start NX/NY/NZ-383-383-383
NX/NY/NZ768768768
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS260260260
D min/max/mean-0.1950.316-0.000

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Supplemental data

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Sample components

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Entire : Yeast apo RNA polymerase I*

EntireName: Yeast apo RNA polymerase I*
Components
  • Complex: Yeast apo RNA polymerase I*
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA190
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA135
    • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC1
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA14
    • 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 I subunit RPA43
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA12
    • 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
  • Ligand: ZINC ION

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Supramolecule #1: Yeast apo RNA polymerase I*

SupramoleculeName: Yeast apo RNA polymerase I* / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#12
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)

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Macromolecule #1: DNA-directed RNA polymerase I subunit RPA190

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA190 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 186.676969 KDa
SequenceString: MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY DLALGAFLRN LCSTCGLDEK FCPGHQGHIE LPVPCYNPL FFNQLYIYLR ASCLFCHHFR LKSVEVHRYA CKLRLLQYGL IDESYKLDEI TLGSLNSSMY TDDEAIEDNE D EMDGEGSK ...String:
MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY DLALGAFLRN LCSTCGLDEK FCPGHQGHIE LPVPCYNPL FFNQLYIYLR ASCLFCHHFR LKSVEVHRYA CKLRLLQYGL IDESYKLDEI TLGSLNSSMY TDDEAIEDNE D EMDGEGSK QSKDISSTLL NELKSKRSEY VDMAIAKALS DGRTTERGSF TATVNDERKK LVHEFHKKLL SRGKCDNCGM FS PKFRKDG FTKIFETALN EKQITNNRVK GFIRQDMIKK QKQAKKLDGS NEASANDEES FDVGRNPTTR PKTGSTYILS TEV KNILDT VFRKEQCVLQ YVFHSRPNLS RKLVKADSFF MDVLVVPPTR FRLPSKLGEE VHENSQNQLL SKVLTTSLLI RDLN DDLSK LQKDKVSLED RRVIFSRLMN AFVTIQNDVN AFIDSTKAQG RTSGKVPIPG VKQALEKKEG LFRKHMMGKR VNYAA RSVI SPDPNIETNE IGVPPVFAVK LTYPEPVTAY NIAELRQAVI NGPDKWPGAT QIQNEDGSLV SLIGMSVEQR KALANQ LLT PSSNVSTHTL NKKVYRHIKN RDVVLMNRQP TLHKASMMGH KVRVLPNEKT LRLHYANTGA YNADFDGDEM NMHFPQN EN ARAEALNLAN TDSQYLTPTS GSPVRGLIQD HISAGVWLTS KDSFFTREQY QQYIYGCIRP EDGHTTRSKI VTLPPTIF K PYPLWTGKQI ITTVLLNVTP PDMPGINLIS KNKIKNEYWG KGSLENEVLF KDGALLCGIL DKSQYGASKY GIVHSLHEV YGPEVAAKVL SVLGRLFTNY ITATAFTCGM DDLRLTAEGN KWRTDILKTS VDTGREAAAE VTNLDKDTPA DDPELLKRLQ EILRDNNKS GILDAVTSSK VNAITSQVVS KCVPDGTMKK FPCNSMQAMA LSGAKGSNVN VSQIMCLLGQ QALEGRRVPV M VSGKTLPS FKPYETDAMA GGYVKGRFYS GIKPQEYYFH CMAGREGLID TAVKTSRSGY LQRCLTKQLE GVHVSYDNSI RD ADGTLVQ FMYGGDAIDI TKESHMTQFE FCLDNYYALL KKYNPSALIE HLDVESALKY SKKTLKYRKK HSKEPHYKQS VKY DPVLAK YNPAKYLGSV SENFQDKLES FLDKNSKLFK SSDGVNEKKF RALMQLKYMR SLINPGEAVG IIASQSVGEP STQM TLNTF HFAGHGAANV TLGIPRLREI VMTASAAIKT PQMTLPIWND VSDEQADTFC KSISKVLLSE VIDKVIVTET TGTSN TAGG NAARSYVIHM RFFDNNEYSE EYDVSKEELQ NVISNQFIHL LEAAIVKEIK KQKRTTGPDI GVAVPRLQTD VANSSS NSK RLEEDNDEEQ SHKKTKQAVS YDEPDEDEIE TMREAEKSSD EEGIDSDKES DSDSEDEDVD MNEQINKSIV EANNNMN KV QRDRQSAIIS HHRFITKYNF DDESGKWCEF KLELAADTEK LLMVNIVEEI CRKSIIRQIP HIDRCVHPEP ENGKRVLV T EGVNFQAMWD QEAFIDVDGI TSNDVAAVLK TYGVEAARNT IVNEINNVFS RYAISVSFRH LDLIADMMTR QGTYLAFNR QGMETSTSSF MKMSYETTCQ FLTKAVLDNE REQLDSPSAR IVVGKLNNVG TGSFDVLAKV PNAA

UniProtKB: DNA-directed RNA polymerase I subunit RPA190

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Macromolecule #2: DNA-directed RNA polymerase I subunit RPA135

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA135 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 135.910328 KDa
SequenceString: MSKVIKPPGQ ARTADFRTLE RESRFINPPK DKSAFPLLQE AVQPHIGSFN ALTEGPDGGL LNLGVKDIGE KVIFDGKPLN SEDEISNSG YLGNKLSVSV EQVSIAKPMS NDGVSSAVER KVYPSESRQR LTSYRGKLLL KLKWSVNNGE ENLFEVRDCG G LPVMLQSN ...String:
MSKVIKPPGQ ARTADFRTLE RESRFINPPK DKSAFPLLQE AVQPHIGSFN ALTEGPDGGL LNLGVKDIGE KVIFDGKPLN SEDEISNSG YLGNKLSVSV EQVSIAKPMS NDGVSSAVER KVYPSESRQR LTSYRGKLLL KLKWSVNNGE ENLFEVRDCG G LPVMLQSN RCHLNKMSPY ELVQHKEESD EIGGYFIVNG IEKLIRMLIV QRRNHPMAII RPSFANRGAS YSHYGIQIRS VR PDQTSQT NVLHYLNDGQ VTFRFSWRKN EYLVPVVMIL KALCHTSDRE IFDGIIGNDV KDSFLTDRLE LLLRGFKKRY PHL QNRTQV LQYLGDKFRV VFQASPDQSD LEVGQEVLDR IVLVHLGKDG SQDKFRMLLF MIRKLYSLVA GECSPDNPDA TQHQ EVLLG GFLYGMILKE KIDEYLQNII AQVRMDINRG MAINFKDKRY MSRVLMRVNE NIGSKMQYFL STGNLVSQSG LDLQQ VSGY TVVAEKINFY RFISHFRMVH RGSFFAQLKT TTVRKLLPES WGFLCPVHTP DGSPCGLLNH FAHKCRISTQ QSDVSR IPS ILYSLGVAPA SHTFAAGPSL CCVQIDGKII GWVSHEQGKI IADTLRYWKV EGKTPGLPID LEIGYVPPST RGQYPGL YL FGGHSRMLRP VRYLPLDKED IVGPFEQVYM NIAVTPQEIQ NNVHTHVEFT PTNILSILAN LTPFSDFNQS PRNMYQCQ M GKQTMGTPGV ALCHRSDNKL YRLQTGQTPI VKANLYDDYG MDNFPNGFNA VVAVISYTGY DMDDAMIINK SADERGFGY GTMYKTEKVD LALNRNRGDP ITQHFGFGND EWPKEWLEKL DEDGLPYIGT YVEEGDPICA YFDDTLNKTK IKTYHSSEPA YIEEVNLIG DESNKFQELQ TVSIKYRIRR TPQIGDKFSS RHGQKGVCSR KWPTIDMPFS ETGIQPDIII NPHAFPSRMT I GMFVESLA GKAGALHGIA QDSTPWIFNE DDTPADYFGE QLAKAGYNYH GNEPMYSGAT GEELRADIYV GVVYYQRLRH MV NDKFQVR STGPVNSLTM QPVKGRKRHG GIRVGEMERD ALIGHGTSFL LQDRLLNSSD YTQASVCREC GSILTTQQSV PRI GSISTV CCRRCSMRFE DAKKLLTKSE DGEKIFIDDS QIWEDGQGNK FVGGNETTTV AIPFVLKYLD SELSAMGIRL RYNV EPK

UniProtKB: DNA-directed RNA polymerase I subunit RPA135

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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: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 37.732613 KDa
SequenceString: MSNIVGIEYN RVTNTTSTDF PGFSKDAENE WNVEKFKKDF EVNISSLDAR EANFDLINID TSIANAFRRI MISEVPSVAA EYVYFFNNT SVIQDEVLAH RIGLVPLKVD PDMLTWVDSN LPDDEKFTDE NTIVLSLNVK CTRNPDAPKG STDPKELYNN A HVYARDLK ...String:
MSNIVGIEYN RVTNTTSTDF PGFSKDAENE WNVEKFKKDF EVNISSLDAR EANFDLINID TSIANAFRRI MISEVPSVAA EYVYFFNNT SVIQDEVLAH RIGLVPLKVD PDMLTWVDSN LPDDEKFTDE NTIVLSLNVK CTRNPDAPKG STDPKELYNN A HVYARDLK FEPQGRQSTT FADCPVVPAD PDILLAKLRP GQEISLKAHC ILGIGGDHAK FSPVSTASYR LLPQINILQP IK GESARRF QKCFPPGVIG IDEGSDEAYV KDARKDTVSR EVLRYEEFAD KVKLGRVRNH FIFNVESAGA MTPEEIFFKS VRI LKNKAE YLKNCPITQ

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

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Macromolecule #4: DNA-directed RNA polymerase I subunit RPA14

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA14 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 14.599128 KDa
SequenceString:
MMKGSRRTGN NTATTLNTPV VIHATQLPQH VSTDEVLQFL ESFIDEKENI IDSTTMNTIS GNAADADAAA VANTSLNIDT NLSSSISQL KRIQRDFKGL PPAQDFSAAP IQVSTTEKKE TSIGVSATGG KKTTFADE

UniProtKB: DNA-directed RNA polymerase I subunit RPA14

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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: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 25.117094 KDa
SequenceString: MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVG VKTMKTFVIH IQEKNFQTGI FVYQNNITPS AMKLVPSIPP ATIETFNEAA LVVNITHHEL VPKHIRLSSD E KRELLKRY ...String:
MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVG VKTMKTFVIH IQEKNFQTGI FVYQNNITPS AMKLVPSIPP ATIETFNEAA LVVNITHHEL VPKHIRLSSD E KRELLKRY RLKESQLPRI QRADPVALYL GLKRGEVVKI IRKSETSGRY ASYRICM

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: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 17.931834 KDa
SequenceString:
MSDYEEAFND GNENFEDFDV EHFSDEETYE EKPQFKDGET TDANGKTIVT GGNGPEDFQQ HEQIRRKTLK EKAIPKDQRA TTPYMTKYE RARILGTRAL QISMNAPVFV DLEGETDPLR IAMKELAEKK IPLVIRRYLP DGSFEDWSVE ELIVDL

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

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Macromolecule #7: DNA-directed RNA polymerase I subunit RPA43

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA43 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 36.264852 KDa
SequenceString: MSQVKRANEN RETARFIKKH KKQVTNPIDE KNGTSNCIVR VPIALYVSLA PMYLENPLQG VMKQHLNPLV MKYNNKVGGV VLGYEGLKI LDADPLSKED TSEKLIKITP DTPFGFTWCH VNLYVWQPQV GDVLEGYIFI QSASHIGLLI HDAFNASIKK N NIPVDWTF ...String:
MSQVKRANEN RETARFIKKH KKQVTNPIDE KNGTSNCIVR VPIALYVSLA PMYLENPLQG VMKQHLNPLV MKYNNKVGGV VLGYEGLKI LDADPLSKED TSEKLIKITP DTPFGFTWCH VNLYVWQPQV GDVLEGYIFI QSASHIGLLI HDAFNASIKK N NIPVDWTF VHNDVEEDAD VINTDENNGN NNNEDNKDSN GGSNSLGKFS FGNRSLGHWV DSNGEPIDGK LRFTVRNVHT TG RVVSVDG TLISDADEEG NGYNSSRSQA ESLPIVSNKK IVFDDEVSIE NKESHKELDL PEVKEDNGSE IVYEENTSES NDG ESSDSD

UniProtKB: DNA-directed RNA polymerase I subunit RPA43

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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: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 16.525363 KDa
SequenceString:
MSNTLFDDIF QVSEVDPGRY NKVCRIEAAS TTQDQCKLTL DINVELFPVA AQDSLTVTIA SSLNLEDTPA NDSSATRSWR PPQAGDRSL ADDYDYVMYG TAYKFEEVSK DLIAVYYSFG GLLMRLEGNY RNLNNLKQEN AYLLIRR

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

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Macromolecule #9: DNA-directed RNA polymerase I subunit RPA12

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA12 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 13.676566 KDa
SequenceString:
MSVVGSLIFC LDCGDLLENP NAVLGSNVEC SQCKAIYPKS QFSNLKVVTT TADDAFPSSL RAKKSVVKTS LKKNELKDGA TIKEKCPQC GNEEMNYHTL QLRSADEGAT VFYTCTSCGY KFRTNN

UniProtKB: DNA-directed RNA polymerase I subunit RPA12

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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: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 8.290732 KDa
SequenceString:
MIVPVRCFSC GKVVGDKWES YLNLLQEDEL DEGTALSRLG LKRYCCRRMI LTHVDLIEKF LRYNPLEKRD

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

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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: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 16.16786 KDa
SequenceString:
MTEDIEQKKT ATEVTPQEPK HIQEEEEQDV DMTGDEEQEE EPDREKIKLL TQATSEDGTS ASFQIVEEDH TLGNALRYVI MKNPDVEFC GYSIPHPSEN LLNIRIQTYG ETTAVDALQK GLKDLMDLCD VVESKFTEKI KSM

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: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 7.729969 KDa
SequenceString:
MSREGFQIPT NLDAAAAGTS QARTATLKYI CAECSSKLSL SRTDAVRCKD CGHRILLKAR TKRLVQFEAR

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

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Macromolecule #13: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 13 / Number of copies: 7 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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

Concentration0.1 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
Details: 30 seconds incubation 3 seconds blotting blotting force 3.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 39.0 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: PDB ENTRY
PDB model - PDB ID:

5m5x

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.21 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2) / Number images used: 73660
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

4c3i

source_name: PDB, initial_model_type: experimental model

4c2m

source_name: PDB, initial_model_type: experimental model
DetailsInitial rigid body fitting was done in Chimera and model building was done in Coot.
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-6hls:
Yeast apo RNA polymerase I*

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