5y6m | pdb_00005y6m

Zika virus helicase in complex with ADP-AlF3

spinqualitylabelsall models 5y6m, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5y6m is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, AF3, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A140GMI3_ZIKV] Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[SAAS:SAAS00892720] Publication Abstract from PubMed During its life cycle, Zika virus (ZIKV), an arthropod-borne flavivirus that is associated with Guillain-Barre syndrome and causes microencephaly in fetuses and newborn children, encodes a critical and indispensable helicase domain that has 5'-triphosphatase activity and performs ATP hydrolysis to generate energy and thus, sustains unwinding of double-stranded RNA during ZIKV genome replication. Of these processes, ATP hydrolysis represents the most basic event; however, its dynamic mechanisms remain largely unknown, impeding the further understanding of the function of ZIKV helicase and the ongoing anti-ZIKV drug design. In this work, we determined the crystal structure of ZIKV helicase in complex with ADP-AlF3-Mn(2+) and ADP-Mn(2+) separately. The structural analysis indicates that these structures represent the intermediate state and posthydrolysis state, respectively, of the ATP hydrolysis process of ZIKV helicase. These findings, together with our earlier work, which identified the prehydrolysis state of ZIKV helicase, lead to a proposal of the ATP hydrolysis cycle for ZIKV helicase. On this basis, we used site-directed mutagenesis combined with an enzymatic study to identify successfully residues that are critical for the ATPase activity of ZIKV helicase; this will provide new ideas to understand the function for the key enzyme of ZIKV.-Yang, X., Chen, C., Tian, H., Chi, H., Mu, Z., Zhang, T., Yang, K., Zhao, Q., Liu, X., Wang, Z., Ji, X., Yang, H. Mechanism of ATP hydrolysis by the Zika virus helicase. Mechanism of ATP hydrolysis by the Zika virus helicase.,Yang X, Chen C, Tian H, Chi H, Mu Z, Zhang T, Yang K, Zhao Q, Liu X, Wang Z, Ji X, Yang H FASEB J. 2018 Apr 17:fj201701140R. doi: 10.1096/fj.201701140R. PMID:29913559 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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