View source for 5wwp


==Crystal structure of Middle East respiratory syndrome coronavirus helicase (MERS-CoV nsp13)==
<StructureSection load='5wwp' size='340' side='right'caption='[[5wwp]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wwp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betacoronavirus_2c_EMC/2012 Human betacoronavirus 2c EMC/2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WWP 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5wwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wwp OCA], [https://pdbe.org/5wwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wwp RCSB], [https://www.ebi.ac.uk/pdbsum/5wwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wwp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K0BWD0_MERS K0BWD0_MERS] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Middle East respiratory syndrome coronavirus (MERS-CoV) remains a threat to public health worldwide; however, effective vaccine or drug against CoVs remains unavailable. CoV helicase is one of the three evolutionary most conserved proteins in nidoviruses, thus making it an important target for drug development. We report here the first structure of full-length coronavirus helicase, MERS-CoV nsp13. MERS-CoV helicase has multiple domains, including an N-terminal Cys/His rich domain (CH) with three zinc atoms, a beta-barrel domain and a C-terminal SF1 helicase core with two RecA-like subdomains. Our structural analyses show that while the domain organization of nsp13 is conserved throughout nidoviruses, the individual domains of nsp13 are closely related to the equivalent eukaryotic domains of Upf1 helicases. The most distinctive feature differentiating CoV helicases from eukaryotic Upf1 helicases is the interaction between CH domain and helicase core.

Crystal structure of Middle East respiratory syndrome coronavirus helicase.,Hao W, Wojdyla JA, Zhao R, Han R, Das R, Zlatev I, Manoharan M, Wang M, Cui S PLoS Pathog. 2017 Jun 26;13(6):e1006474. doi: 10.1371/journal.ppat.1006474., eCollection 2017 Jun. PMID:28651017<ref>PMID:28651017</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wwp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human betacoronavirus 2c EMC/2012]]
[[Category: Large Structures]]
[[Category: Cui S]]
[[Category: Das R]]
[[Category: Han R]]
[[Category: Hao W]]
[[Category: Manoharan M]]
[[Category: Wang M]]
[[Category: Wojdyla JA]]
[[Category: Zhao R]]
[[Category: Zlatev I]]