6AIC
Crystal structures of the N-terminal domain of Staphylococcus aureus DEAD-box Cold shock RNA helicase CshA in complex with AMP
Summary for 6AIC
| Entry DOI | 10.2210/pdb6aic/pdb |
| Related | 6AIB |
| Descriptor | DEAD-box ATP-dependent RNA helicase CshA, ADENOSINE MONOPHOSPHATE (3 entities in total) |
| Functional Keywords | structural protein |
| Biological source | Staphylococcus aureus subsp. aureus MRSA252 |
| Total number of polymer chains | 1 |
| Total formula weight | 24156.01 |
| Authors | Tian, T.,Chengliang, W.,Xiaobao, C.,Xuan, Z.,Jianye, Z. (deposition date: 2018-08-22, release date: 2018-11-21, Last modification date: 2024-03-27) |
| Primary citation | 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 Cited by 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: 30387775DOI: 10.1107/S2053230X1801292X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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