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 -