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Structure. 2011 Dec 7;19(12):1885-94. doi: 10.1016/j.str.2011.09.012.

Structural conservation of the myoviridae phage tail sheath protein fold.

Author information

1
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-2032, USA.

Abstract

Bacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 Å diameter icosahedral head and a 2000 Å-long contractile tail. The structure of the whole virus was previously reported, showing that its tail organization in the extended state is similar to the well-studied Myovirus bacteriophage T4 tail. The crystal structure of a tail sheath protein fragment of phiKZ was determined to 2.4 Å resolution. Furthermore, crystal structures of two prophage tail sheath proteins were determined to 1.9 and 3.3 Å resolution. Despite low sequence identity between these proteins, all of these structures have a similar fold. The crystal structure of the phiKZ tail sheath protein has been fitted into cryo-electron-microscopy reconstructions of the extended tail sheath and of a polysheath. The structural rearrangement of the phiKZ tail sheath contraction was found to be similar to that of phage T4.

PMID:
22153511
PMCID:
PMC3256926
DOI:
10.1016/j.str.2011.09.012
[Indexed for MEDLINE]
Free PMC Article

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