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-Structure paper
タイトル | Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 116, Issue 42, Page 21037-21046, Year 2019 |
掲載日 | 2019年10月15日 |
著者 | Alexis Huet / Robert L Duda / Pascale Boulanger / James F Conway / |
PubMed 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. |
リンク | Proc Natl Acad Sci U S A / PubMed:31578255 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.8 - 7.2 Å |
構造データ | EMDB-20099, PDB-6okb: EMDB-20122, PDB-6oma: EMDB-20123: EMDB-20125, PDB-6omc: |
由来 |
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キーワード | VIRUS LIKE PARTICLE / procapsid / HK97-fold / dsDNA-phage / icosahedral / VIRUS / capsid |