3SPE

Crystal structure of the tail sheath protein protease resistant fragment from bacteriophage phiKZ

Summary for 3SPE

• Entry DOI: 10.2210/pdb3spe/pdb
• Related: 3HXL 3J0H 3J0I 3LML
• Descriptor: PHIKZ029, PHOSPHATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: structural protein
• Biological source: Pseudomonas phage phiKZ
• Total number of polymer chains: 2
• Total formula weight: 65344.80

Authors

Aksyuk, A.A.,Kurochkina, L.P.,Fokine, A.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 2011-07-01, release date: 2011-12-14, Last modification date: 2024-10-30)

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

X-RAY DIFFRACTION (2.3996 Å)