6TUT image
Deposition Date 2020-01-08
Release Date 2020-02-19
Last Version Date 2024-05-22
Entry Detail
PDB ID:
6TUT
Keywords:
TRANSCRIPTION
Title:
Cryo-EM structure of the RNA Polymerase III-Maf1 complex
Biological Source:
Source Organism(s):
Saccharomyces cerevisiae S288C (Taxon ID: 559292)
Expression System(s):
Escherichia coli
Method Details:
Experimental Method:
ELECTRON MICROSCOPY
Resolution:
3.25 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
6TUT validation report missing
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPO31
Chain IDs:A
Chain Length:1460
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P04051 Pfam ID:PF04983, PF05000, PF04998, PF04997, PF00623 EC:2.7.7.6
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RET1
Chain IDs:B
Chain Length:1149
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P22276 Pfam ID:PF04563, PF04561, PF04565, PF04566, PF04567, PF00562, PF04560 EC:2.7.7.6
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPC40
Chain IDs:C
Chain Length:335
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P07703 Pfam ID:PF01193, PF01000
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPC17
Chain IDs:D
Chain Length:161
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P47076 Pfam ID:PF03874
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPB5
Chain IDs:E
Chain Length:215
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P20434 Pfam ID:PF03871, PF01191
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPO26
Chain IDs:F
Chain Length:155
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P20435 Pfam ID:PF01192
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPC25
Chain IDs:G
Chain Length:212
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P35718 Pfam ID:PF03876, PF08292
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPB8
Chain IDs:H
Chain Length:146
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P20436 Pfam ID:PF03870
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPC11
Chain IDs:I
Chain Length:110
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:Q04307 Pfam ID:PF02150, PF01096
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPB10
Chain IDs:J
Chain Length:70
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P22139 Pfam ID:PF01194
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPC19
Chain IDs:K
Chain Length:142
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P28000 Pfam ID:PF13656
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPC10
Chain IDs:L
Chain Length:70
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P40422 Pfam ID:PF03604
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPC37
Chain IDs:M
Chain Length:282
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P36121 Pfam ID:PF04801
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPC53
Chain IDs:N
Chain Length:422
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P25441 Pfam ID:PF05132
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPC82
Chain IDs:O
Chain Length:654
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P32349 Pfam ID:PF22536, PF08221, PF05645, PF20912
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPC34
Chain IDs:P
Chain Length:317
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P32910 Pfam ID:PF05158
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPC31
Chain IDs:Q
Chain Length:251
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P17890 Pfam ID:PF11705
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Repressor of RNA polymerase I
Gene (Uniprot):MAF1
Chain IDs:R
Chain Length:267
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae S288C
UniProt ID:P41910 Pfam ID:PF09174
Ligand Molecules
ZN
Primary Citation
Structural basis for RNA polymerase III transcription repression by Maf1.
Nat. Struct. Mol. Biol. 27 229 232 (2020)
PMID: 32066962 DOI: 10.1038/s41594-020-0383-y

Abstact

Maf1 is a conserved inhibitor of RNA polymerase III (Pol III) that influences phenotypes ranging from metabolic efficiency to lifespan. Here, we present a 3.3-Å-resolution cryo-EM structure of yeast Maf1 bound to Pol III, establishing that Maf1 sequesters Pol III elements involved in transcription initiation and binds the mobile C34 winged helix 2 domain, sealing off the active site. The Maf1 binding site overlaps with that of TFIIIB in the preinitiation complex.

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Primary Citation of related structures
6TUT
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