6otf: Difference between revisions

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'''Unreleased structure'''


The entry 6otf is ON HOLD  until Paper Publication
==Symmetric reconstruction of human norovirus GII.2 Snow Mountain Virus Strain VLP in T=3 symmetry==
<StructureSection load='6otf' size='340' side='right'caption='[[6otf]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6otf]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OTF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OTF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<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=6otf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6otf OCA], [http://pdbe.org/6otf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6otf RCSB], [http://www.ebi.ac.uk/pdbsum/6otf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6otf ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6otf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Diehnelt, C W]]
[[Category: Grant, T]]
[[Category: Grigorieff, N]]
[[Category: Joshua-Tor, L]]
[[Category: Jung, J]]
[[Category: Thomas, D R]]
[[Category: Caliciviridae]]
[[Category: Gii 2]]
[[Category: Norovirus]]
[[Category: Snow mountain virus]]
[[Category: Virus like particle]]

Revision as of 06:59, 26 June 2019

Symmetric reconstruction of human norovirus GII.2 Snow Mountain Virus Strain VLP in T=3 symmetry

6otf, resolution 3.10Å

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