Molecular architecture of the prolate head of bacteriophage T4

Andrei Fokine, Paul R. Chipman, Petr G. Leiman, Vadim V. Mesyanzhinov, Venigalla B. Rao, Michael G. Rossmann

Research output: Contribution to journalArticle

213 Scopus citations

Abstract

The head of bacteriophage T4 is a prolate icosahedron with one unique portal vertex to which the phage tail is attached. The three-dimensional structure of mature bacteriophage T4 head has been determined to 22-Å resolution by using cryo-electron microscopy. The T4 capsid has a hexagonal surface lattice characterized by the triangulation numbers Tend = 13 laevo for the icosahedral caps and Tmid = 20 for the midsection. Hexamers of the major capsid protein gene product (gp)23* and pentamers of the vertex protein gp24*, as well as the outer surface proteins highly antigenic outer capsid protein (hoc) and small outer capsid protein (soc), are clearly evident in the reconstruction. The size and shape of the gp23* hexamers are similar to the major capsid protein organization of bacteriophage HK97. The binding sites and shape of the hoc and soc proteins have been established by analysis of the soc- and hoc-soc - T4 structures.

Original languageEnglish (US)
Pages (from-to)6003-6008
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number16
DOIs
StatePublished - Apr 20 2004

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