|Title||Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy.|
|Journal, issue, pages||Proc. Natl. Acad. Sci. U.S.A., Year 2019|
|Publish date||Oct 2, 2019|
|Authors||Alexis Huet / Robert L Duda / Pascale Boulanger / James F Conway /|
|PubMed Abstract||The large (90-nm) icosahedral capsid of bacteriophage T5 is composed of 775 copies of the major capsid protein (mcp) together with portal, protease, and decoration proteins. Its assembly is a ...The large (90-nm) icosahedral capsid of bacteriophage T5 is composed of 775 copies of the major capsid protein (mcp) together with portal, protease, and decoration proteins. Its assembly is a regulated process that involves several intermediates, including a thick-walled round precursor prohead that expands as the viral DNA is packaged to yield a thin-walled and angular mature capsid. We investigated capsid maturation by comparing cryoelectron microscopy (cryo-EM) structures of the prohead, the empty expanded capsid both with and without decoration protein, and the virion capsid at a resolution of 3.8 Å for the latter. We detail the molecular structure of the mcp, its complex pattern of interactions, and their evolution during maturation. The bacteriophage T5 mcp is a variant of the canonical HK97-fold with a high level of plasticity that allows for the precise assembly of a giant macromolecule and the adaptability needed to interact with other proteins and the packaged DNA.|
|External links||PubMed:31578255 / Publisher's page|
|Keywords||VIRUS LIKE PARTICLE / procapsid / HK97-fold / dsDNA-phage / icosahedral / VIRUS / capsid|
|Methods||EM (single particle, icos. sym.) / EM (single particle)|
|Resolution||3.8 - 7.2 A|
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