PDBsum entry 4aby

Hydrolase

PDB id: 4aby

Contents

Protein chains

358 a.a.

311 a.a.

Waters ×102

PDB id:

4aby

Name:

Hydrolase

Title:

Crystal structure of deinococcus radiodurans recn head domain

Structure:

DNA repair protein recn. Chain: a, b, c, d. Fragment: head domain, residues 1-195,365-564. Synonym: recn, recombination protein n. Engineered: yes

Source:

Deinococcus radiodurans. Organism_taxid: 243230. Strain: r1. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: star.

Resolution:

3.00Å R-factor: 0.212 R-free: 0.249

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:

12-Dec-11 Release date: 12-Dec-12

Protein chains

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: 564 a.a.

Struc: 358 a.a.*

Protein chain

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: 564 a.a.

Struc: 311 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.3.6.1.3 - Deleted entry.
• Reaction: ATP + H₂O = 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 using a combination of protein crystallography and small-angle X-ray scattering enabled us to assemble 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.