title: Crystal structure of Deinococcus radiodurans RecQ helicase catalytic core domain: the interdomain flexibility.
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.
authors.affiliation: Department of Biotechnology, Hungkuang University, Taichung 433, Taiwan ; Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City 221, Taiwan.
authors.forename: Sheng-Chia
authors.initials: SC
authors.lastname: Chen
authors.affiliation: Department of Biotechnology, Hungkuang University, Taichung 433, Taiwan ; Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City 221, Taiwan ; Institute of Biochemistry, National Chung-Hsing University, Taichung 40227, Taiwan.
authors.forename: Chi-Hung
authors.identifier: 0000-0002-8887-4962
authors.initials: CH
authors.lastname: Huang
authors.affiliation: Department of Biotechnology, Hungkuang University, Taichung 433, Taiwan ; Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City 221, Taiwan.
authors.forename: Chia Shin
authors.initials: CS
authors.lastname: Yang
authors.affiliation: Department of Biological Science and Technology, College of Life Sciences, China Medical University, Taichung 40402, Taiwan.
authors.forename: Tzong-Der
authors.initials: TD
authors.lastname: Way
authors.affiliation: Department of Nutrition, Hungkuang University, Taichung 433, Taiwan.
authors.forename: Ming-Chung
authors.initials: MC
authors.lastname: Chang
authors.affiliation: Department of Biotechnology, Hungkuang University, Taichung 433, Taiwan.
authors.forename: Yeh
authors.identifier: 0000-0002-7740-0446
authors.initials: Y
authors.lastname: Chen
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D034301:Deinococcus / Q000201:enzymology*; D008969:Molecular Sequence Data; D053484:RecQ Helicases / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity; D040681:Structural Homology, Protein
chemical_list: D000244:Adenosine Diphosphate; D053484:RecQ Helicases