PDBsum entry 4q48

DNA binding protein

PDB id: 4q48

Contents

Protein chains

500 a.a.

Metals

_ZN ×2

PDB id:

4q48

Name:

DNA binding protein

Title:

Structure of the recq catalytic core from deinococcus radiodurans

Structure:

DNA helicase recq. Chain: a, b. Fragment: unp residues 1-517. Engineered: yes

Source:

Deinococcus radiodurans. Organism_taxid: 243230. Strain: atcc 13939 / dsm 20539 / jcm 16871 / lmg 4051 / nbrc 15346 / ncimb 9279 / r1 / vkm b-1422. Gene: dr_1289. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.80Å R-factor: 0.218 R-free: 0.286

Authors:

S.C.Chen,C.S.Yang,Y.Chen

Key ref:

S.C.Chen et al. (2014). Crystal structure of Deinococcus radiodurans RecQ helicase catalytic core domain: the interdomain flexibility. Biomed Res Int, 2014, 342725. PubMed id: 25243132 DOI: 10.1155/2014/342725

Date:

14-Apr-14 Release date: 20-May-15

Protein chains

Q9RUU2  (Q9RUU2_DEIRA) -  DNA helicase RecQ from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

Seq: 824 a.a.

Struc: 500 a.a.

Enzyme reactions

• Enzyme class: E.C.5.6.2.4 - Dna 3'-5' helicase.

DOI no: 10.1155/2014/342725

Biomed Res Int 2014:342725 (2014)

PubMed id: 25243132

Crystal structure of Deinococcus radiodurans RecQ helicase catalytic core domain: the interdomain flexibility.

S.C.Chen, C.H.Huang, C.S.Yang, T.D.Way, M.C.Chang, Y.Chen.

ABSTRACT

RecQ DNA helicases are key enzymes in the maintenance of genome integrity, and they have functions in DNA replication, recombination, and repair. In contrast to most RecQs, RecQ from Deinococcus radiodurans (DrRecQ) possesses an unusual domain architecture that is crucial for its remarkable ability to repair DNA. Here, we determined the crystal structures of the DrRecQ helicase catalytic core and its ADP-bound form, revealing interdomain flexibility in its first RecA-like and winged-helix (WH) domains. Additionally, the WH domain of DrRecQ is positioned in a different orientation from that of the E. coli RecQ (EcRecQ). These results suggest that the orientation of the protein during DNA-binding is significantly different when comparing DrRecQ and EcRecQ.