View source for 5gjc


==Zika virus NS3 helicase in complex with ATP==
<StructureSection load='5gjc' size='340' side='right'caption='[[5gjc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gjc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zika_virus Zika virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GJC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.204&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gjc OCA], [https://pdbe.org/5gjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gjc RCSB], [https://www.ebi.ac.uk/pdbsum/5gjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gjc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0U4DG08_ZIKV A0A0U4DG08_ZIKV] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The recent explosive outbreak of Zika virus (ZIKV) infection has been reported in South and Central America and the Caribbean. Neonatal microcephaly associated with ZIKV infection has already caused a public health emergency of international concern. No specific vaccines or drugs are currently available to treat ZIKV infection. The ZIKV helicase, which plays a pivotal role in viral RNA replication, is an attractive target for therapy. We determined the crystal structures of ZIKV helicase-ATP-Mn2+ and ZIKV helicase-RNA. This is the first structure of any flavivirus helicase bound to ATP. Comparisons with related flavivirus helicases have shown that although the critical P-loop in the active site has variable conformations among different species, it adopts an identical mode to recognize ATP/Mn2+. The structure of ZIKV helicase-RNA has revealed that upon RNA binding, rotations of the motor domains can cause significant conformational changes. Strikingly, although ZIKV and dengue virus (DENV) apo-helicases share conserved residues for RNA binding, their different manners of motor domain rotations result in distinct individual modes for RNA recognition. It suggests that flavivirus helicases could have evolved a conserved engine to convert chemical energy from nucleoside triphosphate to mechanical energy for RNA unwinding, but different motor domain rotations result in variable RNA recognition modes to adapt to individual viral replication.

Structural basis of Zika virus helicase in recognizing its substrates.,Tian H, Ji X, Yang X, Zhang Z, Lu Z, Yang K, Chen C, Zhao Q, Chi H, Mu Z, Xie W, Wang Z, Lou H, Yang H, Rao Z Protein Cell. 2016 Jul 18. PMID:27430951<ref>PMID:27430951</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gjc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
*[[Virus protease 3D structures|Virus protease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zika virus]]
[[Category: Chen C]]
[[Category: Chi H]]
[[Category: Ji XY]]
[[Category: Lou HQ]]
[[Category: Lu ZK]]
[[Category: Mu ZY]]
[[Category: Rao ZH]]
[[Category: Tian HL]]
[[Category: Wang ZF]]
[[Category: Xie W]]
[[Category: Yang HT]]
[[Category: Yang KL]]
[[Category: Yang XY]]
[[Category: Zhang ZX]]
[[Category: Zhao Q]]