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- W2896683941 abstract "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 CshA R1 ) and of its complex with AMP ( Sa CshA R1 –AMP) are reported at resolutions of 1.5 and 1.8 Å, respectively. Sa CshA 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 Sa CshA R1 –AMP and Sa CshA R1 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 Sa CshA compared with other DEAD-box RNA helicases." @default.
- W2896683941 created "2018-10-26" @default.
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- W2896683941 date "2018-10-16" @default.
- W2896683941 modified "2023-10-17" @default.
- W2896683941 title "Crystal structures of the N-terminal domain of the <i>Staphylococcus aureus</i> DEAD-box RNA helicase CshA and its complex with AMP" @default.
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- W2896683941 doi "https://doi.org/10.1107/s2053230x1801292x" @default.
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