ArticleBioMed research international2014
Crystal structure of Deinococcus radiodurans RecQ helicase catalytic core domain: the interdomain flexibility.
Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Efficient coordination between the winged helix domain and the aromatic-rich loop restructures the ATPase domain and facilitates DNA unwinding by human RECQ1.Nucleic acids research · 2025Article
- RecQ helicases in DNA repair and cancer targets.Essays in biochemistry · 2020Review
- Structural features and functional implications of proteins enabling the robustness ofComputational and structural biotechnology journal · 2020Review
- Insights into the RecQ helicase mechanism revealed by the structure of the helicase domain of human RECQL5.Nucleic acids research · 2017Article
- A Decade of Biochemical and Structural Studies of the DNA Repair Machinery ofComputational and structural biotechnology journal · 2016Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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