6zty

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Current revision (09:49, 2 April 2025) (edit) (undo)
 
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==Assembly intermediates of orthoreovirus captured in the cell==
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<StructureSection load='6zty' size='340' side='right'caption='[[6zty]]' scene=''>
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<StructureSection load='6zty' size='340' side='right'caption='[[6zty]], [[Resolution|resolution]] 5.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6zty]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZTY FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zty OCA], [http://pdbe.org/6zty PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zty RCSB], [http://www.ebi.ac.uk/pdbsum/6zty PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zty ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.6&#8491;</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=6zty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zty OCA], [https://pdbe.org/6zty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zty RCSB], [https://www.ebi.ac.uk/pdbsum/6zty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zty ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MU1_REOVL MU1_REOVL] Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell.<ref>PMID:11007773</ref> <ref>PMID:15280481</ref> <ref>PMID:16912293</ref> <ref>PMID:17005655</ref> <ref>PMID:18369316</ref> The viral outer shell polypeptides, of which mu-1 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.<ref>PMID:11007773</ref> <ref>PMID:15280481</ref> <ref>PMID:16912293</ref> <ref>PMID:17005655</ref> <ref>PMID:18369316</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Traditionally, molecular assembly pathways for viruses are inferred from high resolution structures of purified stable intermediates, low resolution images of cell sections and genetic approaches. Here, we directly visualise an unsuspected 'single shelled' intermediate for a mammalian orthoreovirus in cryo-preserved infected cells, by cryo-electron tomography of cellular lamellae. Particle classification and averaging yields structures to 5.6 A resolution, sufficient to identify secondary structural elements and produce an atomic model of the intermediate, comprising 120 copies each of protein lambda1 and sigma2. This lambda1 shell is 'collapsed' compared to the mature virions, with molecules pushed inwards at the icosahedral fivefolds by ~100 A, reminiscent of the first assembly intermediate of certain prokaryotic dsRNA viruses. This supports the supposition that these viruses share a common ancestor, and suggests mechanisms for the assembly of viruses of the Reoviridae. Such methodology holds promise for dissecting the replication cycle of many viruses.
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Assembly intermediates of orthoreovirus captured in the cell.,Sutton G, Sun D, Fu X, Kotecha A, Hecksel CW, Clare DK, Zhang P, Stuart DI, Boyce M Nat Commun. 2020 Sep 7;11(1):4445. doi: 10.1038/s41467-020-18243-9. PMID:32895380<ref>PMID:32895380</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6zty" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Reovirus sp]]
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[[Category: Stuart DI]]
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[[Category: Sutton GC]]

Current revision

Assembly intermediates of orthoreovirus captured in the cell

PDB ID 6zty

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