6jdu: Difference between revisions
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<StructureSection load='6jdu' size='340' side='right'caption='[[6jdu]], [[Resolution|resolution]] 2.81Å' scene=''> | <StructureSection load='6jdu' size='340' side='right'caption='[[6jdu]], [[Resolution|resolution]] 2.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jdu]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6jdu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Porcine_reproductive_and_respiratory_syndrome_virus Porcine reproductive and respiratory syndrome virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JDU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.81Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6jdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jdu OCA], [https://pdbe.org/6jdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jdu RCSB], [https://www.ebi.ac.uk/pdbsum/6jdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jdu ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/J9XNG9_PRRSV J9XNG9_PRRSV] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6jdu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6jdu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Nonstructural protein 3D structures|Nonstructural protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Porcine reproductive and respiratory syndrome virus]] | ||
[[Category: Chen | [[Category: Chen Z]] | ||
[[Category: Tang | [[Category: Tang C]] | ||
Latest revision as of 13:07, 22 November 2023
Crystal structure of PRRSV nsp10 (helicase)Crystal structure of PRRSV nsp10 (helicase)
Structural highlights
FunctionPublication Abstract from PubMedPorcine reproductive and respiratory syndrome virus (PRRSV) is prevalent throughout the world and has caused great economic losses to the swine industry. Nonstructural protein 10 (nsp10) is a superfamily 1 helicase participating in multiple processes of virus replication and one of the three most conserved proteins in nidoviruses. Here we report three high resolution crystal structures of highly pathogenic PRRSV nsp10. PRRSV nsp10 has multiple domains, including an N-terminal zinc-binding domain (ZBD), a beta-barrel domain, a helicase core with two RecA-like domains, and a C-terminal domain (CTD). The CTD adopts a novel fold and is required for the overall structure and enzymatic activities. Although each domain except the CTD aligns well with its homologs, PRRSV nsp10 adopts an unexpected extended overall structure in crystals and solution. Moreover, structural and functional analyses of PRRSV nsp10 versus its closest homolog, equine arteritis virus nsp10, suggest that DNA binding might induce a profound conformational change of PRRSV nsp10 to exert functions, thus shedding light on the mechanisms of activity regulation of this helicase. Helicase of Type 2 Porcine Reproductive and Respiratory Syndrome Virus Strain HV Reveals a Unique Structure.,Tang C, Deng Z, Li X, Yang M, Tian Z, Chen Z, Wang G, Wu W, Feng WH, Zhang G, Chen Z Viruses. 2020 Feb 14;12(2). pii: v12020215. doi: 10.3390/v12020215. PMID:32075207[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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