National Institutes of Health/National Human Genome Research Institute
R01 GM047795
米国
National Institutes of Health/National Human Genome Research Institute
S10 OD019995
米国
引用
ジャーナル: Proc Natl Acad Sci U S A / 年: 2019 タイトル: Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy. 著者: Alexis Huet / Robert L Duda / Pascale Boulanger / James F Conway / 要旨: 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.