8c38: Difference between revisions
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==Contracted cowpea chlorotic mottle virus== | |||
<StructureSection load='8c38' size='340' side='right'caption='[[8c38]], [[Resolution|resolution]] 1.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8c38]] 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=8C38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C38 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]] 1.64Å</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=8c38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c38 OCA], [https://pdbe.org/8c38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c38 RCSB], [https://www.ebi.ac.uk/pdbsum/8c38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c38 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8c38" 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 17:04, 18 October 2023
Contracted cowpea chlorotic mottle virusContracted cowpea chlorotic mottle virus
Structural highlights
FunctionCAPSD_CCMV Capsid protein. Probably binds RNA and plays a role in packaging.[1] Publication Abstract from PubMedObserving 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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