8cpy: Difference between revisions

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'''Unreleased structure'''


The entry 8cpy is ON HOLD  until Paper Publication
==Extended cowpea chlorotic mottle virus==
<StructureSection load='8cpy' size='340' side='right'caption='[[8cpy]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cpy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cowpea_chlorotic_mottle_virus Cowpea chlorotic mottle virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CPY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CPY 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]] 3.9&#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=8cpy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cpy OCA], [https://pdbe.org/8cpy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cpy RCSB], [https://www.ebi.ac.uk/pdbsum/8cpy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cpy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_CCMV CAPSD_CCMV] Capsid protein. Probably binds RNA and plays a role in packaging.<ref>PMID:15731222</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Observing proteins as they perform their tasks has largely remained elusive, which has left our understanding of protein function fundamentally incomplete. To enable such observations, we have recently proposed a technique that improves the time resolution of cryo-electron microscopy (cryo-EM) to microseconds. Here, we demonstrate that microsecond time-resolved cryo-EM enables observations of fast protein dynamics. We use our approach to elucidate the mechanics of the capsid of cowpea chlorotic mottle virus (CCMV), whose large-amplitude motions play a crucial role in the viral life cycle. We observe that a pH jump causes the extended configuration of the capsid to contract on the microsecond timescale. While this is a concerted process, the motions of the capsid proteins involve different timescales, leading to a curved reaction path. It is difficult to conceive how such a detailed picture of the dynamics could have been obtained with any other method, which highlights the potential of our technique. Crucially, our experiments pave the way for microsecond time-resolved cryo-EM to be applied to a broad range of protein dynamics that previously could not have been observed. This promises to fundamentally advance our understanding of protein function.


Authors:  
Fast viral dynamics revealed by microsecond time-resolved cryo-EM.,Harder OF, Barrass SV, Drabbels M, Lorenz UJ Nat Commun. 2023 Sep 13;14(1):5649. doi: 10.1038/s41467-023-41444-x. PMID:37704664<ref>PMID:37704664</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 8cpy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cowpea chlorotic mottle virus]]
[[Category: Large Structures]]
[[Category: Barrass SV]]
[[Category: Drabbels M]]
[[Category: Harder OF]]
[[Category: Lorenz UJ]]

Latest revision as of 06:54, 27 September 2023

Extended cowpea chlorotic mottle virus

8cpy, resolution 3.90Å

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