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3iyu
From Proteopedia
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| - | [[ | + | ==Atomic model of an infectious rotavirus particle== |
| + | <StructureSection load='3iyu' size='340' side='right' caption='[[3iyu]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3iyu]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Simian_rotavirus_a Simian rotavirus a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IYU FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n09|3n09]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3iyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iyu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3iyu RCSB], [http://www.ebi.ac.uk/pdbsum/3iyu PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Non-enveloped viruses of different types have evolved distinct mechanisms for penetrating a cellular membrane during infection. Rotavirus penetration appears to occur by a process resembling enveloped-virus fusion: membrane distortion linked to conformational changes in a viral protein. Evidence for such a mechanism comes from crystallographic analyses of fragments of VP4, the rotavirus-penetration protein, and infectivity analyses of structure-based VP4 mutants. We describe here the structure of an infectious rotavirus particle determined by electron cryomicroscopy (cryoEM) and single-particle analysis at about 4.3 A resolution. The cryoEM image reconstruction permits a nearly complete trace of the VP4 polypeptide chain, including the positions of most side chains. It shows how the two subfragments of VP4 (VP8(*) and VP5(*)) retain their association after proteolytic cleavage, reveals multiple structural roles for the beta-barrel domain of VP5(*), and specifies interactions of VP4 with other capsid proteins. The virion model allows us to integrate structural and functional information into a coherent mechanism for rotavirus entry. | ||
| - | + | Atomic model of an infectious rotavirus particle.,Settembre EC, Chen JZ, Dormitzer PR, Grigorieff N, Harrison SC EMBO J. 2011 Jan 19;30(2):408-16. Epub 2010 Dec 14. PMID:21157433<ref>PMID:21157433</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Simian rotavirus a]] | [[Category: Simian rotavirus a]] | ||
[[Category: Chen, J Z.]] | [[Category: Chen, J Z.]] | ||
Revision as of 09:51, 21 May 2014
Atomic model of an infectious rotavirus particle
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