View source for 9jmg


==Cryo-EM structure of EU-HedgehogCoV (Erinaceus/VMC/DEU/2012) S-trimer in a locked-2 conformation==
<StructureSection load='9jmg' size='340' side='right'caption='[[9jmg]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jmg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Betacoronavirus_Erinaceus/VMC/DEU/2012 Betacoronavirus Erinaceus/VMC/DEU/2012] and [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9JMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JMG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=9jmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jmg OCA], [https://pdbe.org/9jmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jmg RCSB], [https://www.ebi.ac.uk/pdbsum/9jmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jmg ProSAT]</span></td></tr>
</table>
== Function ==
[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/U5LMM7_9BETC U5LMM7_9BETC] Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099]  Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099]  Spike protein S2: 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]
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</StructureSection>
[[Category: Betacoronavirus Erinaceus/VMC/DEU/2012]]
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Xiong X]]
[[Category: Yuan H]]