Crystal structures of the N-terminal domain of the Staphylococcus aureus DEAD-box RNA helicase CshA and its complex with AMP.

ABSTRACT: CshA is a DEAD-box RNA helicase that belongs to the DExD/H-box family of proteins, which generally have an RNA-dependent ATPase activity. In Staphylococcus aureus, CshA was identified as a component of the RNA degradosome and plays important roles in RNA turnover. In this study, the crystal structures of the N-terminal RecA-like domain 1 of S. aureus CshA (SaCshA^R1) and of its complex with AMP (SaCshA^R1-AMP) are reported at resolutions of 1.5 and 1.8 Å, respectively. SaCshA^R1 adopts a conserved α/β RecA-like structure with seven parallel strands surrounded by nine α-helices. The Q motif and motif I are responsible for the binding of the adenine group and phosphate group of AMP, respectively. Structure comparison of SaCshA^R1-AMP and SaCshA^R1<

SUBMITTER: Chen X 

PROVIDER: S-EPMC6213976 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature