Crystal structures of the N‐terminal domain of the Staphylococcus aureus DEAD‐box RNA helicase CshA and its complex with AMP
作者: Xiaobao ChenChengliang WangXuan ZhangTian TianJianye Zang
作者单位: 1Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, Collaborative Innovation Center of Chemistry for Life Science, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui230026, People's Republic of China
2 Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui230027, People's Republic of China
刊名: Acta Crystallographica Section F, 2018, Vol.74 (11), pp.704-709
来源数据库: Wiley Journal
DOI: 10.1107/S2053230X1801292X
关键词: CshADEAD‐box RNA helicaseAMPCrystallography
原始语种摘要: CshA is a DEAD‐box RNA helicase that belongs to the DE x D/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 ( Sa CshAR1) and of its complex with AMP ( Sa CshAR1–AMP) are reported at resolutions of 1.5 and 1.8 Å, respectively. Sa CshAR1 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 Sa CshAR1–AMP and Sa...
全文获取路径: Wiley  (合作)

  • helicase 蜗牛酶
  • AMP Amperage
  • domain 领域
  • complex 超群
  • motif 花纹图案
  • binding 装订
  • further 进一步
  • adenine 腺嘌呤
  • seven