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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.

SUBMITTER: Chen SC

PROVIDER: S-EPMC4163472 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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

Chen Sheng-Chia SC Huang Chi-Hung CH Yang Chia Shin CS Way Tzong-Der TD Chang Ming-Chung MC Chen Yeh Y

BioMed research international 20140827

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) d ...[more]

PMID: 25243132

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Expression, purification, crystallization and preliminary X-ray analysis of the RecQ helicase catalytic core from Deinococcus radiodurans.

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