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PDBsum entry 4a93

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protein dna_rna metals Protein-protein interface(s) links
Transcription PDB id
4a93
Jmol
Contents
Protein chains
1422 a.a.
1113 a.a.
266 a.a.
178 a.a.
214 a.a.
84 a.a.
171 a.a.
133 a.a.
119 a.a.
65 a.a.
115 a.a.
46 a.a.
DNA/RNA
Metals
_MG
_ZN ×8
PDB id:
4a93
Name: Transcription
Title: RNA polymerase ii elongation complex containing a cpd lesion
Structure: DNA-directed RNA polymerase ii subunit rpb1. Chain: a. Fragment: residues 1-1732. Synonym: rpb1, RNA polymerase ii subunit 1, RNA polymerase subunit b1, DNA-directed RNA polymerase iii largest subuni polymerase ii subunit b220. DNA-directed RNA polymerase ii subunit rpb2. Chain: b. Synonym: rpb2, RNA polymerase ii subunit 2, b150, DNA-direc
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Synthetic: yes. Organism_taxid: 4932
Resolution:
3.40Å     R-factor:   0.165     R-free:   0.198
Authors: C.Walmacq,A.C.M.Cheung,M.L.Kireeva,L.Lubkowska,C.Ye,D.Gotte, J.N.Strathern,T.Carell,P.Cramer,M.Kashlev
Key ref: C.Walmacq et al. (2012). Mechanism of translesion transcription by RNA polymerase II and its role in cellular resistance to DNA damage. Mol Cell, 46, 18-29. PubMed id: 22405652 DOI: 10.1016/j.molcel.2012.02.006
Date:
23-Nov-11     Release date:   21-Mar-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04050  (RPB1_YEAST) -  DNA-directed RNA polymerase II subunit RPB1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1733 a.a.
1422 a.a.
Protein chain
Pfam   ArchSchema ?
P08518  (RPB2_YEAST) -  DNA-directed RNA polymerase II subunit RPB2
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1224 a.a.
1113 a.a.*
Protein chain
Pfam   ArchSchema ?
P16370  (RPB3_YEAST) -  DNA-directed RNA polymerase II subunit RPB3
Seq:
Struc:
318 a.a.
266 a.a.
Protein chain
Pfam   ArchSchema ?
P20433  (RPB4_YEAST) -  DNA-directed RNA polymerase II subunit RPB4
Seq:
Struc:
221 a.a.
178 a.a.
Protein chain
Pfam   ArchSchema ?
P20434  (RPAB1_YEAST) -  DNA-directed RNA polymerases I, II, and III subunit RPABC1
Seq:
Struc:
215 a.a.
214 a.a.
Protein chain
Pfam   ArchSchema ?
P20435  (RPAB2_YEAST) -  DNA-directed RNA polymerases I, II, and III subunit RPABC2
Seq:
Struc:
155 a.a.
84 a.a.
Protein chain
Pfam   ArchSchema ?
P34087  (RPB7_YEAST) -  DNA-directed RNA polymerase II subunit RPB7
Seq:
Struc:
171 a.a.
171 a.a.
Protein chain
Pfam   ArchSchema ?
P20436  (RPAB3_YEAST) -  DNA-directed RNA polymerases I, II, and III subunit RPABC3
Seq:
Struc:
146 a.a.
133 a.a.
Protein chain
Pfam   ArchSchema ?
P27999  (RPB9_YEAST) -  DNA-directed RNA polymerase II subunit RPB9
Seq:
Struc:
122 a.a.
119 a.a.
Protein chain
Pfam   ArchSchema ?
P22139  (RPAB5_YEAST) -  DNA-directed RNA polymerases I, II, and III subunit RPABC5
Seq:
Struc:
70 a.a.
65 a.a.
Protein chain
Pfam   ArchSchema ?
P38902  (RPB11_YEAST) -  DNA-directed RNA polymerase II subunit RPB11
Seq:
Struc:
120 a.a.
115 a.a.
Protein chain
Pfam   ArchSchema ?
P40422  (RPAB4_YEAST) -  DNA-directed RNA polymerases I, II, and III subunit RPABC4
Seq:
Struc:
70 a.a.
46 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.2.7.7.6  - DNA-directed Rna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Nucleoside triphosphate
+ RNA(n)
= diphosphate
+ RNA(n+1)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   8 terms 
  Biological process     transcription, RNA-dependent   22 terms 
  Biochemical function     RNA polymerase II activity     20 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.molcel.2012.02.006 Mol Cell 46:18-29 (2012)
PubMed id: 22405652  
 
 
Mechanism of translesion transcription by RNA polymerase II and its role in cellular resistance to DNA damage.
C.Walmacq, A.C.Cheung, M.L.Kireeva, L.Lubkowska, C.Ye, D.Gotte, J.N.Strathern, T.Carell, P.Cramer, M.Kashlev.
 
  ABSTRACT  
 
No abstract given.