Structural highlights
Publication Abstract from PubMed
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.
Crystal structure of Deinococcus radiodurans RecQ helicase catalytic core domain: the interdomain flexibility.,Chen SC, Huang CH, Yang CS, Way TD, Chang MC, Chen Y Biomed Res Int. 2014;2014:342725. doi: 10.1155/2014/342725. Epub 2014 Aug 27. PMID:25243132[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen SC, Huang CH, Yang CS, Way TD, Chang MC, Chen Y. Crystal structure of Deinococcus radiodurans RecQ helicase catalytic core domain: the interdomain flexibility. Biomed Res Int. 2014;2014:342725. doi: 10.1155/2014/342725. Epub 2014 Aug 27. PMID:25243132 doi:http://dx.doi.org/10.1155/2014/342725
