3J0I

Fitting of the phiKZ gp29PR structure into the cryo-EM density map of the phiKZ polysheath

Summary for 3J0I

• Entry DOI: 10.2210/pdb3j0i/pdb
• Related: 3HXL 3J0H 3LML 3SPE
• EMDB information: 5331 5332
• Descriptor: PHIKZ029 (1 entity in total)
• Functional Keywords: bacteriophage tail sheath, structural protein
• Biological source: Pseudomonas phage phiKZ
• Total number of polymer chains: 6
• Total formula weight: 193781.46

Authors

Aksyuk, A.A.,Fokine, A.,Kurochkina, L.P.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 2011-08-16, release date: 2011-12-14, Last modification date: 2024-02-21)

Primary citation

Aksyuk, A.A.,Kurochkina, L.P.,Fokine, A.,Forouhar, F.,Mesyanzhinov, V.V.,Tong, L.,Rossmann, M.G.
Structural conservation of the myoviridae phage tail sheath protein fold.
Structure, 19:1885-1894, 2011

PubMed 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.

PubMed: 22153511
DOI: 10.1016/j.str.2011.09.012

Experimental method

ELECTRON MICROSCOPY (19 Å)