4jgs

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{{STRUCTURE_4jgs| PDB=4jgs | SCENE= }}
 
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===Crystal structure of the xmrv tm retroviral fusion core===
 
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{{ABSTRACT_PUBMED_24131724}}
 
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==Function==
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==Crystal structure of the xmrv tm retroviral fusion core==
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[[http://www.uniprot.org/uniprot/ENV1_MOUSE ENV1_MOUSE]] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 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. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
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<StructureSection load='4jgs' size='340' side='right'caption='[[4jgs]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4jgs]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JGS FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4jgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jgs OCA], [https://pdbe.org/4jgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jgs RCSB], [https://www.ebi.ac.uk/pdbsum/4jgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jgs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/D0UFA8_9GAMR D0UFA8_9GAMR]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Membrane fusion is a key step in the life cycle of all envelope viruses, but this process is energetically unfavorable; the transmembrane fusion subunit (TM) of the virion-attached glycoprotein actively catalyzes the membrane merger process. Retroviral glycoproteins are the prototypical system to study pH-independent viral entry. In this study, we determined crystal structures of extramembrane regions of the TMs from Mason-Pfizer monkey virus (MPMV) and xenotropic murine leukemia virus-related virus (XMRV) at 1.7-A and 2.2-A resolution, respectively. The structures are comprised of a trimer of hairpins that is characteristic of class I viral fusion proteins and now completes a structural library of retroviral fusion proteins. Our results allowed us to identify a series of intra- and interchain electrostatic interactions in the heptad repeat and chain reversal regions. Mutagenesis reveals that charge-neutralizing salt bridge mutations significantly destabilize the postfusion six-helix bundle and abrogate retroviral infection, demonstrating that electrostatic stapling of the fusion subunit is essential for viral entry. Our data indicate that salt bridges are a major stabilizing force on the MPMV and XMRV retroviral TMs and likely provide the key energetics for viral and host membrane fusion.
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==About this Structure==
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Crystal structures of Beta- and gammaretrovirus fusion proteins reveal a role for electrostatic stapling in viral entry.,Aydin H, Cook JD, Lee JE J Virol. 2014 Jan;88(1):143-53. doi: 10.1128/JVI.02023-13. Epub 2013 Oct 16. PMID:24131724<ref>PMID:24131724</ref>
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[[4jgs]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JGS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024131724</ref><references group="xtra"/><references/>
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</div>
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[[Category: Lk3 transgenic mice]]
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<div class="pdbe-citations 4jgs" style="background-color:#fffaf0;"></div>
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[[Category: Aydin, H.]]
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== References ==
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[[Category: Cook, J D.]]
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<references/>
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[[Category: Lee, J E.]]
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__TOC__
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[[Category: Six helix bundle]]
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</StructureSection>
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[[Category: Viral protein]]
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[[Category: Large Structures]]
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[[Category: Viral surface]]
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[[Category: Mus musculus]]
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[[Category: Viral-host membrane fusion]]
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[[Category: Aydin H]]
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[[Category: Xmrv tm]]
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[[Category: Cook JD]]
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[[Category: Lee JE]]

Current revision

Crystal structure of the xmrv tm retroviral fusion core

PDB ID 4jgs

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