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==The limits of structural plasticity in a picornavirus capsid revealed by a massively expanded equine rhinitis A virus particle==
<SX load='4ctg' size='340' side='right' viewer='molstar' caption='[[4ctg]], [[Resolution|resolution]] 17.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ctg]] is a 180 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_rhinitis_A_virus Equine rhinitis A virus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d14 4d14], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d15 4d15], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d16 4d16] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d2a 4d2a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CTG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 17&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ctg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ctg OCA], [https://pdbe.org/4ctg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ctg RCSB], [https://www.ebi.ac.uk/pdbsum/4ctg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ctg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B9VV85_9PICO B9VV85_9PICO] 
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== Publication Abstract from PubMed ==
The Picornaviridae family of small, nonenveloped viruses includes major pathogens of humans and animals. They have positive-sense, single-stranded RNA genomes, and the mechanism(s) by which these genomes are introduced into cells to initiate infection remains poorly understood. The structures of presumed uncoating intermediate particles of several picornaviruses show limited expansion and some increased porosity compared to the mature virions. Here, we present the cryo-electron microscopy structure of native equine rhinitis A virus (ERAV), together with the structure of a massively expanded ERAV particle, each at approximately 17-A resolution. The expanded structure has large pores on the particle 3-fold axes and has lost the RNA genome and the capsid protein VP4. The expanded structure thus illustrates both the limits of structural plasticity in such capsids and a plausible route by which genomic RNA might exit. IMPORTANCE: Picornaviruses are important animal and human pathogens that protect their genomic RNAs within a protective protein capsid. Upon infection, this genomic RNA must be able to leave the capsid to initiate a new round of infection. We describe here the structure of a unique, massively expanded state of equine rhinitis A virus that provides insight into how this exit might occur.

Limits of structural plasticity in a picornavirus capsid revealed by a massively expanded equine rhinitis a virus particle.,Bakker SE, Groppelli E, Pearson AR, Stockley PG, Rowlands DJ, Ranson NA J Virol. 2014 Jun;88(11):6093-9. doi: 10.1128/JVI.01979-13. Epub 2014 Mar 19. PMID:24648455<ref>PMID:24648455</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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[[Category: Equine rhinitis A virus]]
[[Category: Large Structures]]
[[Category: Bakker SE]]
[[Category: Groppelli E]]
[[Category: Pearson AR]]
[[Category: Ranson NA]]
[[Category: Rowlands DJ]]
[[Category: Stockley PG]]