TY - JOUR A2 - Huang, Cheng-Yang AU - Chen, Sheng-Chia AU - Huang, Chi-Hung AU - Yang, Chia Shin AU - Way, Tzong-Der AU - Chang, Ming-Chung AU - Chen, Yeh PY - 2014 DA - 2014/08/27 TI - Crystal Structure of Deinococcus radiodurans RecQ Helicase Catalytic Core Domain: The Interdomain Flexibility SP - 342725 VL - 2014 AB - 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. SN - 2314-6133 UR - https://doi.org/10.1155/2014/342725 DO - 10.1155/2014/342725 JF - BioMed Research International PB - Hindawi Publishing Corporation KW - ER -