5k8l | pdb_00005k8l

Apo structure

spinqualitylabelsall models 5k8l, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5k8l is a 1 chain structure with sequence from Zikv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, EDO, GSP, MPD Related: 5jwh, 5k8i, 5k8t, 5k8u Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Zika virus has attracted increasing attention because of its potential for causing human neural disorders, including microcephaly in infants and Guillain-Barre syndrome. Its NS3 helicase domain plays critical roles in NTP-dependent RNA unwinding and translocation during viral replication. Our structural analysis revealed a pre-activation state of NS3 helicase in complex with GTPgammaS, in which the triphosphate adopts a compact conformation in the absence of any divalent metal ions. In contrast, in the presence of a divalent cation, GTPgammaS adopts an extended conformation, and the Walker A motif undergoes substantial conformational changes. Both features contribute to more extensive interactions between the GTPgammaS and the enzyme. Thus, this study provides structural evidence on the allosteric modulation of MgNTP(2-) on the NS3 helicase activity. Furthermore, the compact conformation of inhibitory NTP identified in this study provides precise information for the rational drug design of small molecule inhibitors for the treatment of ZIKV infection. Molecular mechanism of divalent-metal-induced activation of NS3 helicase and insights into Zika virus inhibitor design.,Cao X, Li Y, Jin X, Li Y, Guo F, Jin T Nucleic Acids Res. 2016 Dec 1;44(21):10505-10514. doi: 10.1093/nar/gkw941. Epub, 2016 Oct 19. PMID:27915293 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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