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1YUE

Bacteriophage T4 capsid vertex protein gp24

Summary for 1YUE
Entry DOI10.2210/pdb1yue/pdb
DescriptorHead vertex protein Gp24 (1 entity in total)
Functional Keywordsgp24, bacteriophage t4, capsid protein, vertex, bacteriophage, virus, hk97, mad, viral protein
Biological sourceEnterobacteria phage T4
Cellular locationVirion (Potential): P19896
Total number of polymer chains1
Total formula weight47273.50
Authors
Fokine, A.,Leiman, P.G.,Shneider, M.M.,Ahvazi, B.,Boeshans, K.M.,Steven, A.C.,Black, L.W.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 2005-02-14, release date: 2005-04-26, Last modification date: 2024-11-13)
Primary citationFokine, A.,Leiman, P.G.,Shneider, M.M.,Ahvazi, B.,Boeshans, K.M.,Steven, A.C.,Black, L.W.,Mesyanzhinov, V.V.,Rossmann, M.G.
Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry.
Proc.Natl.Acad.Sci.Usa, 102:7163-7168, 2005
Cited by
PubMed Abstract: Gene product (gp) 24 of bacteriophage T4 forms the pentameric vertices of the capsid. Using x-ray crystallography, we found the principal domain of gp24 to have a polypeptide fold similar to that of the HK97 phage capsid protein plus an additional insertion domain. Fitting gp24 monomers into a cryo-EM density map of the mature T4 capsid suggests that the insertion domain interacts with a neighboring subunit, effecting a stabilization analogous to the covalent crosslinking in the HK97 capsid. Sequence alignment and genetic data show that the folds of gp24 and the hexamer-forming capsid protein, gp23*, are similar. Accordingly, models of gp24* pentamers, gp23* hexamers, and the whole capsid were built, based on a cryo-EM image reconstruction of the capsid. Mutations in gene 23 that affect capsid shape map to the capsomer's periphery, whereas mutations that allow gp23 to substitute for gp24 at the vertices modify the interactions between monomers within capsomers. Structural data show that capsid proteins of most tailed phages, and some eukaryotic viruses, may have evolved from a common ancestor.
PubMed: 15878991
DOI: 10.1073/pnas.0502164102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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