5k8t
From Proteopedia
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<StructureSection load='5k8t' size='340' side='right' caption='[[5k8t]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='5k8t' size='340' side='right' caption='[[5k8t]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5k8t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K8T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k8t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Zikv Zikv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K8T FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jwh|5jwh]], [[5k8i|5k8i]], [[5k8l|5k8l]], [[5k8u|5k8u]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jwh|5jwh]], [[5k8i|5k8i]], [[5k8l|5k8l]], [[5k8u|5k8u]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k8t OCA], [http://pdbe.org/5k8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k8t RCSB], [http://www.ebi.ac.uk/pdbsum/5k8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k8t ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k8t OCA], [http://pdbe.org/5k8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k8t RCSB], [http://www.ebi.ac.uk/pdbsum/5k8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k8t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:27915293</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5k8t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Zikv]] | ||
[[Category: Cao, X]] | [[Category: Cao, X]] | ||
[[Category: Jin, T]] | [[Category: Jin, T]] | ||
Revision as of 07:38, 6 December 2017
Crystal structure of ZIKV NS3 helicase in complex with GTP-gammar S and an magnesium ion
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