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PDBsum entry 4ad8

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protein links
DNA binding protein PDB id
4ad8

 

 

 

 

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Contents
Protein chain
452 a.a.
PDB id:
4ad8
Name: DNA binding protein
Title: Crystal structure of a deletion mutant of deinococcus radiodurans recn
Structure: DNA repair protein recn. Chain: a. Fragment: head and partial coiled-coil domains, residues 1-237,305- 564. Synonym: recombination protein n, recn. Engineered: yes
Source: Deinococcus radiodurans. Organism_taxid: 243230. Strain: r1. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: star.
Resolution:
4.00Å     R-factor:   0.326     R-free:   0.347
Authors: S.Pellegrino,J.Radzimanowski,D.De Sanctis,S.Mcsweeney,J.Timmins
Key ref: S.Pellegrino et al. (2012). Structural and functional characterization of an SMC-like protein RecN: new insights into double-strand break repair. Structure, 20, 2076-2089. PubMed id: 23085075
Date:
22-Dec-11     Release date:   12-Dec-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9WXF2  (RECN_DEIRA) -  DNA repair protein RecN from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Seq:
Struc:
 
Seq:
Struc:
564 a.a.
452 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.6.1.3  - Deleted entry.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate
ATP
+ H(2)O
= ADP
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Structure 20:2076-2089 (2012)
PubMed id: 23085075  
 
 
Structural and functional characterization of an SMC-like protein RecN: new insights into double-strand break repair.
S.Pellegrino, J.Radzimanowski, D.de Sanctis, E.Boeri Erba, S.McSweeney, J.Timmins.
 
  ABSTRACT  
 
Repair of DNA double-strand breaks (DSBs) is essential for cell survival and maintaining genome integrity. DSBs are repaired in a stepwise manner by homologous recombination. Here, we focused on the early steps of DSB repair, including DSB recognition, which is still only poorly understood. In prokaryotes, this process has been proposed to involve the RecN protein, a member of the structural maintenance of chromosome (SMC) protein family, which include key eukaryotic and prokaryotic proteins such as cohesin, condensin, and Rad50. An extensive high- and low-resolution structural analysis of Deinococcus radiodurans RecN usingĀ a combination of protein crystallography and small-angle X-ray scattering enabled us to assembleĀ a quasi-atomic model of the entire RecN protein, representing the complete structure of a SMC-like protein. These results, together with a thorough biochemical and mutational study of RecN, allow us to propose a model for the role of RecN in DSB repair.
 

 

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