title: Structural conservation of the myoviridae phage tail sheath protein fold.
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.
authors.affiliation: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-2032, USA.
authors.forename: Anastasia A
authors.initials: AA
authors.lastname: Aksyuk
authors.forename: Lidia P
authors.initials: LP
authors.lastname: Kurochkina
authors.forename: Andrei
authors.initials: A
authors.lastname: Fokine
authors.forename: Farhad
authors.initials: F
authors.lastname: Forouhar
authors.forename: Vadim V
authors.initials: VV
authors.lastname: Mesyanzhinov
authors.forename: Liang
authors.initials: L
authors.lastname: Tong
authors.forename: Michael G
authors.initials: MG
authors.lastname: Rossmann
mesh_terms: D017122:Bacteriophage T4 / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D008854:Microscopy, Electron; D017900:Myoviridae / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017376:Viral Tail Proteins / Q000737:chemistry*
chemical_list: D017376:Viral Tail Proteins