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PDBsum entry 4ruc

Go to PDB code: 
protein dna_rna ligands metals links
Transferase/DNA PDB id
4ruc

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
341 a.a.
DNA/RNA
Ligands
DTP
Metals
_CA ×3
Waters ×58
PDB id:
4ruc
Name: Transferase/DNA
Title: Crystal structure of y-family DNA polymerase dpo4 extending from a mefapy-dg:dc pair
Structure: DNA polymerase iv. Chain: a. Synonym: pol iv. Engineered: yes. Nucleic acids template: tcat(mf7)taatccttccccc. Chain: t. Engineered: yes. Nucleic acids primar: gggggaaggattac. Chain: p.
Source: Sulfolobus solfataricus p2. Organism_taxid: 273057. Strain: atcc 35092 / dsm 1617 / jcm 11322 / p2. Gene: dbh, dpo4, sso2448. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.
Resolution:
2.90Å     R-factor:   0.175     R-free:   0.236
Authors: A.Patra,S.Banerjee,M.P.Stone,M.Egli
Key ref: A.Patra et al. (2015). Structural Basis for Error-Free Bypass of the 5-N-Methylformamidopyrimidine-dG Lesion by Human DNA Polymerase η and Sulfolobus solfataricus P2 Polymerase IV. J Am Chem Soc, 137, 7011-7014. PubMed id: 25988947 DOI: 10.1021/jacs.5b02701
Date:
18-Nov-14     Release date:   05-Aug-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Q97W02  (DPO4_SULSO) -  DNA polymerase IV from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Seq:
Struc:
352 a.a.
341 a.a.
Key:    Secondary structure  CATH domain

DNA/RNA chains
  C-A-T-MF7-T-A-A-T-C-C-T-T-C-C-C-C-C 17 bases
  G-G-G-G-G-A-A-G-G-A-T-T-A-C 14 bases

 Enzyme reactions 
   Enzyme class: E.C.2.7.7.7  - DNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
DNA(n)
+ 2'-deoxyribonucleoside 5'-triphosphate
= DNA(n+1)
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1021/jacs.5b02701 J Am Chem Soc 137:7011-7014 (2015)
PubMed id: 25988947  
 
 
Structural Basis for Error-Free Bypass of the 5-N-Methylformamidopyrimidine-dG Lesion by Human DNA Polymerase η and Sulfolobus solfataricus P2 Polymerase IV.
A.Patra, S.Banerjee, T.L.Johnson Salyard, C.K.Malik, P.P.Christov, C.J.Rizzo, M.P.Stone, M.Egli.
 
  ABSTRACT  
 
N(6)-(2-Deoxy-d-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine (MeFapy-dG) arises from N7-methylation of deoxyguanosine followed by imidazole ring opening. The lesion has been reported to persist in animal tissues. Previous in vitro replication bypass investigations of the MeFapy-dG adduct revealed predominant insertion of C opposite the lesion, dependent on the identity of the DNA polymerase (Pol) and the local sequence context. Here we report crystal structures of ternary Pol·DNA·dNTP complexes between MeFapy-dG-adducted DNA template:primer duplexes and the Y-family polymerases human Pol η and P2 Pol IV (Dpo4) from Sulfolobus solfataricus. The structures of the hPol η and Dpo4 complexes at the insertion and extension stages, respectively, are representative of error-free replication, with MeFapy-dG in the anti conformation and forming Watson-Crick pairs with dCTP or dC.
 

 

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