6AIB

Crystal structures of the N-terminal RecA-like domain 1 of Staphylococcus aureus DEAD-box Cold shock RNA helicase CshA

6AIB の概要

• エントリーDOI: 10.2210/pdb6aib/pdb
• 分子名称: DEAD-box ATP-dependent RNA helicase CshA (2 entities in total)
• 機能のキーワード: structural protein
• 由来する生物種: Staphylococcus aureus subsp. aureus MRSA252
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23808.79

構造登録者

Chengliang, W.,Tian, T.,Xiaobao, C.,Xuan, Z.,Jianye, Z. (登録日: 2018-08-22, 公開日: 2018-11-21, 最終更新日: 2024-03-27)

主引用文献

Chen, X.,Wang, C.,Zhang, X.,Tian, T.,Zang, J.
Crystal structures of the N-terminal domain of the Staphylococcus aureus DEAD-box RNA helicase CshA and its complex with AMP
Acta Crystallogr F Struct Biol Commun, 74:704-709, 2018

PubMed 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) and of its complex with AMP (SaCshA-AMP) are reported at resolutions of 1.5 and 1.8 Å, respectively. SaCshA 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-AMP and SaCshA reveals that motif I undergoes a conformational change upon AMP binding. Isothermal titration calorimetry assays further conformed the essential roles of Phe22 in the Q motif and Lys52 in motif I for binding ATP, indicating a conserved substrate-binding mechanism in SaCshA compared with other DEAD-box RNA helicases.

PubMed: 30387775
DOI: 10.1107/S2053230X1801292X

実験手法

X-RAY DIFFRACTION (1.5 Å)