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6out

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==Asymmetric focused reconstruction of human norovirus GI.1 Norwalk strain VLP asymmetric unit in T=3 symmetry==
==Asymmetric focused reconstruction of human norovirus GI.1 Norwalk strain VLP asymmetric unit in T=3 symmetry==
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<StructureSection load='6out' size='340' side='right'caption='[[6out]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<SX load='6out' size='340' side='right' viewer='molstar' caption='[[6out]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6out]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OUT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6out]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_Hu/1968/US Norovirus Hu/1968/US]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OUT FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6otf|6otf]]</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]] 2.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6out FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6out OCA], [http://pdbe.org/6out PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6out RCSB], [http://www.ebi.ac.uk/pdbsum/6out PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6out ProSAT]</span></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=6out FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6out OCA], [https://pdbe.org/6out PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6out RCSB], [https://www.ebi.ac.uk/pdbsum/6out PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6out ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CAPSD_NVN68 CAPSD_NVN68]] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.<ref>PMID:16840313</ref> Soluble capsid protein may play a role in viral immunoevasion.<ref>PMID:16840313</ref>
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[https://www.uniprot.org/uniprot/CAPSD_NVN68 CAPSD_NVN68] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.<ref>PMID:16840313</ref> Soluble capsid protein may play a role in viral immunoevasion.<ref>PMID:16840313</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Noroviruses are a leading cause of foodborne illnesses worldwide. Although GII.4 strains have been responsible for most norovirus outbreaks, the assembled virus shell structures have been available in detail for only a single strain (GI.1). We present high-resolution (2.6- to 4.1-A) cryoelectron microscopy (cryo-EM) structures of GII.4, GII.2, GI.7, and GI.1 human norovirus outbreak strain virus-like particles (VLPs). Although norovirus VLPs have been thought to exist in a single-sized assembly, our structures reveal polymorphism between and within genogroups, with small, medium, and large particle sizes observed. Using asymmetric reconstruction, we were able to resolve a Zn(2+) metal ion adjacent to the coreceptor binding site, which affected the structural stability of the shell. Our structures serve as valuable templates for facilitating vaccine formulations.
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High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations.,Jung J, Grant T, Thomas DR, Diehnelt CW, Grigorieff N, Joshua-Tor L Proc Natl Acad Sci U S A. 2019 Jun 10. pii: 1903562116. doi:, 10.1073/pnas.1903562116. PMID:31182604<ref>PMID:31182604</ref>
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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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 6out" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Diehnelt, C W]]
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[[Category: Norovirus Hu/1968/US]]
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[[Category: Grant, T]]
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[[Category: Diehnelt CW]]
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[[Category: Grigorieff, N]]
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[[Category: Grant T]]
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[[Category: Joshua-Tor, L]]
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[[Category: Grigorieff N]]
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[[Category: Jung, J]]
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[[Category: Joshua-Tor L]]
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[[Category: Thomas, D R]]
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[[Category: Jung J]]
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[[Category: Caliciviridae]]
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[[Category: Thomas DR]]
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[[Category: Gi 1]]
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[[Category: Norovirus]]
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[[Category: Norwalk]]
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[[Category: Virus like particle]]
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Current revision

Asymmetric focused reconstruction of human norovirus GI.1 Norwalk strain VLP asymmetric unit in T=3 symmetry

6out, resolution 2.60Å

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