Literature DB >> 22153511

Structural conservation of the myoviridae phage tail sheath protein fold.

Anastasia A Aksyuk1, Lidia P Kurochkina, Andrei Fokine, Farhad Forouhar, Vadim V Mesyanzhinov, Liang Tong, Michael G Rossmann.   

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.
Copyright © 2011 Elsevier Ltd. All rights reserved.

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Year:  2011        PMID: 22153511      PMCID: PMC3256926          DOI: 10.1016/j.str.2011.09.012

Source DB:  PubMed          Journal:  Structure        ISSN: 0969-2126            Impact factor:   5.006


  32 in total

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10.  Investigating the Process of Sheath Maturation in Antifeeding Prophage: a Phage Tail-Like Protein Translocation Structure.

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