Insights into the RecQ helicase mechanism revealed by the structure of the helicase domain of human RECQL5.

ABSTRACT: RecQ helicases are important maintainers of genome integrity with distinct roles in almost every cellular process requiring access to DNA. RECQL5 is one of five human RecQ proteins and is particularly versatile in this regard, forming protein complexes with a diverse set of cellular partners in order to coordinate its helicase activity to various processes including replication, recombination and DNA repair. In this study, we have determined crystal structures of the core helicase domain of RECQL5 both with and without the nucleotide ADP in two distinctly different ('Open' and 'Closed') conformations. Small angle X-ray scattering studies show that the 'Open' form of the protein predominates in solution and we discuss implications of this with regards to the RECQL5 mechanism and conformatio

SUBMITTER: Newman JA 

PROVIDER: S-EPMC5397160 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature