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TitleDeterminants of bacteriophage phi29 head morphology.
Journal, issue, pagesStructure, Vol. 14, Issue 11, Page 1723-1727, Year 2006
Publish dateJan 16, 2007
AuthorsKyung H Choi / Marc C Morais / Dwight L Anderson / Michael G Rossmann /
PubMed AbstractBacteriophage phi29 requires scaffolding protein to assemble the 450 x 540 A prolate prohead with T = 3 symmetry end caps. In infections with a temperature-sensitive mutant scaffolding protein, ...Bacteriophage phi29 requires scaffolding protein to assemble the 450 x 540 A prolate prohead with T = 3 symmetry end caps. In infections with a temperature-sensitive mutant scaffolding protein, capsids assemble predominantly into 370 A diameter isometric particles with T = 3 symmetry that lack a head-tail connector. However, a few larger, 430 A diameter, particles are also assembled. Cryo-electron microscopy shows that these larger particles are icosahedral with T = 4 symmetry. The prolate prohead, as well as the two isometric capsids with T = 3 and T = 4 symmetry, are composed of similar pentamers and differently skewed hexamers. The skewing of the hexamers in the equatorial region of proheads and in the T = 4 isometric particles reflects their different environments. One of the functions of the scaffolding protein, present in the prohead, may be to stabilize skewed hexamers during assembly.
External linksStructure / PubMed:17098197
MethodsEM (single particle)
Resolution20.0 Å
Structure data

EMDB-1281:
Determinants of bacteriophage phi29 head morphology.
Method: EM (single particle) / Resolution: 20.0 Å

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