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6out

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Revision as of 06:35, 10 July 2019

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

Structural highlights

6out is a 3 chain structure with sequence from Hu/nv/nv/1968/us. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	6otf
Gene:	ORF2 (Hu/NV/NV/1968/US)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] Soluble capsid protein may play a role in viral immunoevasion.^[2]

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tan M, Meller J, Jiang X. C-terminal arginine cluster is essential for receptor binding of norovirus capsid protein. J Virol. 2006 Aug;80(15):7322-31. PMID:16840313 doi:http://dx.doi.org/80/15/7322
↑ Tan M, Meller J, Jiang X. C-terminal arginine cluster is essential for receptor binding of norovirus capsid protein. J Virol. 2006 Aug;80(15):7322-31. PMID:16840313 doi:http://dx.doi.org/80/15/7322
↑ Jung J, Grant T, Thomas DR, Diehnelt CW, Grigorieff N, Joshua-Tor L. High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations. Proc Natl Acad Sci U S A. 2019 Jun 10. pii: 1903562116. doi:, 10.1073/pnas.1903562116. PMID:31182604 doi:http://dx.doi.org/10.1073/pnas.1903562116

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6out"

@@ Line 3: / Line 3: @@
 <StructureSection load='6out' size='340' side='right'caption='[[6out]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[6out]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Hu/nv/nv/1968/us Hu/nv/nv/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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OUT FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6otf|6otf]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=524364 Hu/NV/NV/1968/US])</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=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>
 </table>
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Hu/nv/nv/1968/us]]
 [[Category: Large Structures]]
 [[Category: Diehnelt, C W]]

6out

From Proteopedia

Revision as of 06:35, 10 July 2019

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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