3GTG image
Deposition Date 2009-03-27
Release Date 2009-06-09
Last Version Date 2024-11-06
Entry Detail
PDB ID:
3GTG
Title:
Backtracked RNA polymerase II complex with 12mer RNA
Biological Source:
Source Organism(s):
Method Details:
Experimental Method:
Resolution:
3.78 Å
R-Value Free:
0.29
R-Value Work:
0.25
R-Value Observed:
0.25
Space Group:
C 1 2 1
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPO21
Chain IDs:A
Chain Length:1733
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPB2
Chain IDs:B
Chain Length:1224
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPB3
Chain IDs:C
Chain Length:318
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPB5
Chain IDs:D (auth: E)
Chain Length:215
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPO26
Chain IDs:E (auth: F)
Chain Length:155
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPB8
Chain IDs:F (auth: H)
Chain Length:146
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPB9
Chain IDs:G (auth: I)
Chain Length:122
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPB10
Chain IDs:H (auth: J)
Chain Length:70
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerase I
Gene (Uniprot):RPB11
Chain IDs:I (auth: K)
Chain Length:120
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:DNA-directed RNA polymerases
Gene (Uniprot):RPC10
Chain IDs:J (auth: L)
Chain Length:70
Number of Molecules:1
Biological Source:Saccharomyces cerevisiae
Polymer Type:polydeoxyribonucleotide
Molecule:DNA (5'-D(*CP*TP*GP*CP*TP*TP*
Chain IDs:M (auth: N)
Chain Length:14
Number of Molecules:1
Biological Source:
Polymer Type:polyribonucleotide
Molecule:RNA (5'-R(*AP*UP*CP*GP*AP*GP*
Chain IDs:K (auth: R)
Chain Length:12
Number of Molecules:1
Biological Source:
Polymer Type:polydeoxyribonucleotide
Molecule:DNA (28-MER)
Chain IDs:L (auth: T)
Chain Length:29
Number of Molecules:1
Biological Source:
Primary Citation
Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution.
Science 324 1203 1206 (2009)
PMID: 19478184 DOI: 10.1126/science.1168729

Abstact

Transcribing RNA polymerases oscillate between three stable states, two of which, pre- and posttranslocated, were previously subjected to x-ray crystal structure determination. We report here the crystal structure of RNA polymerase II in the third state, the reverse translocated, or "backtracked" state. The defining feature of the backtracked structure is a binding site for the first backtracked nucleotide. This binding site is occupied in case of nucleotide misincorporation in the RNA or damage to the DNA, and is termed the "P" site because it supports proofreading. The predominant mechanism of proofreading is the excision of a dinucleotide in the presence of the elongation factor SII (TFIIS). Structure determination of a cocrystal with TFIIS reveals a rearrangement whereby cleavage of the RNA may take place.

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Disease

Primary Citation of related structures
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