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| Title | Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy. |
|---|---|
| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 116, Issue 42, Page 21037-21046, Year 2019 |
| Publish date | Oct 15, 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 | Proc Natl Acad Sci U S A / PubMed:31578255 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.8 - 7.2 Å |
| Structure data | EMDB-20099, PDB-6okb: EMDB-20122, PDB-6oma:  EMDB-20123: EMDB-20125, PDB-6omc: |
| Source |
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 Keywords | VIRUS LIKE PARTICLE / procapsid / HK97-fold / dsDNA-phage / icosahedral / VIRUS / capsid |
escherichia phage t5 (virus)
