8C38

Contracted cowpea chlorotic mottle virus

Summary for 8C38

• Entry DOI: 10.2210/pdb8c38/pdb
• EMDB information: 16400
• Descriptor: Capsid protein (1 entity in total)
• Functional Keywords: icosahedral, contracted, virus
• Biological source: Cowpea chlorotic mottle virus
• Total number of polymer chains: 3
• Total formula weight: 61098.83

Authors

Harder, O.F.,Barrass, S.V.,Drabbels, M.,Lorenz, U.J. (deposition date: 2022-12-23, release date: 2023-10-18)

Primary citation

Harder, O.F.,Barrass, S.V.,Drabbels, M.,Lorenz, U.J.
Fast viral dynamics revealed by microsecond time-resolved cryo-EM.
Nat Commun, 14:5649-5649, 2023

PubMed Abstract: 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.

PubMed: 37704664
DOI: 10.1038/s41467-023-41444-x

Experimental method

ELECTRON MICROSCOPY (1.64 Å)