6OMC
capsid of T5 virion
Summary for 6OMC
| Entry DOI | 10.2210/pdb6omc/pdb |
| EMDB information | 20099 20122 20123 20125 |
| Descriptor | Major capsid protein (1 entity in total) |
| Functional Keywords | capsid, hk97-fold, dsdna-phage, icosahedral, virus |
| Biological source | Escherichia phage T5 |
| Total number of polymer chains | 13 |
| Total formula weight | 428107.67 |
| Authors | Huet, A.,Duda, R.L.,Boulanger, P.,Conway, J.F. (deposition date: 2019-04-18, release date: 2019-10-02, Last modification date: 2024-03-20) |
| Primary citation | Huet, A.,Duda, R.L.,Boulanger, P.,Conway, J.F. Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy. Proc.Natl.Acad.Sci.USA, 116:21037-21046, 2019 Cited by 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 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. PubMed: 31578255DOI: 10.1073/pnas.1909645116 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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