7zh1

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'''Unreleased structure'''
 
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The entry 7zh1 is ON HOLD until Paper Publication
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==SARS CoV Spike protein, Closed C3 conformation==
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<StructureSection load='7zh1' size='340' side='right'caption='[[7zh1]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7zh1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZH1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zh1 OCA], [https://pdbe.org/7zh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zh1 RCSB], [https://www.ebi.ac.uk/pdbsum/7zh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zh1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').[https://www.uniprot.org/uniprot/SPIKE_SARS SPIKE_SARS] May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity.<ref>PMID:31199522</ref> Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 and CLEC4M/DC-SIGNR receptors and internalization of the virus into the endosomes of the host cell induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membrane fusion within endosomes.[HAMAP-Rule:MF_04099]<ref>PMID:14670965</ref> <ref>PMID:15496474</ref> Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.[HAMAP-Rule:MF_04099] Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099]<ref>PMID:19321428</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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As coronavirus disease 2019 (COVID-19) persists, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) emerge, accumulating spike (S) glycoprotein mutations. S receptor binding domain (RBD) comprises a free fatty acid (FFA)-binding pocket. FFA binding stabilizes a locked S conformation, interfering with virus infectivity. We provide evidence that the pocket is conserved in pathogenic beta-coronaviruses (beta-CoVs) infecting humans. SARS-CoV, MERS-CoV, SARS-CoV-2, and VOCs bind the essential FFA linoleic acid (LA), while binding is abolished by one mutation in common cold-causing HCoV-HKU1. In the SARS-CoV S structure, LA stabilizes the locked conformation, while the open, infectious conformation is devoid of LA. Electron tomography of SARS-CoV-2-infected cells reveals that LA treatment inhibits viral replication, resulting in fewer deformed virions. Our results establish FFA binding as a hallmark of pathogenic beta-CoV infection and replication, setting the stage for FFA-based antiviral strategies to overcome COVID-19.
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Authors:
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The free fatty acid-binding pocket is a conserved hallmark in pathogenic beta-coronavirus spike proteins from SARS-CoV to Omicron.,Toelzer C, Gupta K, Yadav SKN, Hodgson L, Williamson MK, Buzas D, Borucu U, Powers K, Stenner R, Vasileiou K, Garzoni F, Fitzgerald D, Payre C, Gautam G, Lambeau G, Davidson AD, Verkade P, Frank M, Berger I, Schaffitzel C Sci Adv. 2022 Nov 25;8(47):eadc9179. doi: 10.1126/sciadv.adc9179. Epub 2022 Nov , 23. PMID:36417532<ref>PMID:36417532</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 7zh1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia virus T4]]
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[[Category: Large Structures]]
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[[Category: Severe acute respiratory syndrome-related coronavirus]]
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[[Category: Berger I]]
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[[Category: Borucu U]]
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[[Category: Buzas D]]
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[[Category: Gupta K]]
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[[Category: Schaffitzel C]]
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[[Category: Toelzer C]]
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[[Category: Yadav SKN]]

Revision as of 10:25, 15 February 2023

SARS CoV Spike protein, Closed C3 conformation

PDB ID 7zh1

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