AI Article Synopsis
- Bacteriophage T5 has a large 90-nm icosahedral capsid made up of 775 major capsid proteins and other essential proteins, and its assembly involves several intermediates.
- Using cryoelectron microscopy, researchers studied the structures of the prohead, the empty expanded capsid, and the mature virion capsid to understand how capsid maturation occurs.
- The major capsid protein exhibits a unique HK97-fold structure with high plasticity, allowing for effective assembly and interaction with other proteins and viral DNA during maturation.
Article 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 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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6800373 | PMC |
| http://dx.doi.org/10.1073/pnas.1909645116 | DOI Listing |
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