4Q47

Structure of the DrRecQ Catalytic Core in complex with ADP

Summary for 4Q47

• Entry DOI: 10.2210/pdb4q47/pdb
• Related: 1OYW 2V1X 4Q48
• Descriptor: DNA helicase RecQ, ADENOSINE-5'-DIPHOSPHATE, ZINC ION (3 entities in total)
• Functional Keywords: dna unwinding, topoisomerase, helicase, dna binding protein
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 2
• Total formula weight: 117804.27

Authors

Chen, S.C.,Yang, C.S.,Chen, Y. (deposition date: 2014-04-14, release date: 2015-05-20, Last modification date: 2023-11-08)

Primary citation

Chen, S.C.,Huang, C.H.,Yang, C.S.,Way, T.D.,Chang, M.C.,Chen, Y.
Crystal structure of Deinococcus radiodurans RecQ helicase catalytic core domain: the interdomain flexibility.
Biomed Res Int, 2014:342725-342725, 2014

PubMed 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.

PubMed: 25243132
DOI: 10.1155/2014/342725

Experimental method

X-RAY DIFFRACTION (2.899 Å)