Structural Conservation of the Myoviridae Phage Tail Sheath Protein Fold

被引:36
作者
Aksyuk, Anastasia A. [1 ]
Kurochkina, Lidia P. [2 ]
Fokine, Andrei [1 ]
Forouhar, Farhad [3 ]
Mesyanzhinov, Vadim V. [2 ]
Tong, Liang [3 ]
Rossmann, Michael G. [1 ]
机构
[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
[2] Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia
[3] Columbia Univ, NE Struct Genom Consortium, Dept Biol Sci, New York, NY 10027 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
BACTERIOPHAGE-PHI-KZ; DENSITY MODIFICATION; MICROSCOPY; SOFTWARE; CRYSTALLOGRAPHY; RECONSTRUCTION; VISUALIZATION; SYSTEM; HEAD;
D O I
10.1016/j.str.2011.09.012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Bacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 angstrom diameter icosahedral head and a 2000 angstrom-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 angstrom resolution. Furthermore, crystal structures of two prophage tail sheath proteins were determined to 1.9 and 3.3 angstrom 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.
引用
收藏
页码:1885 / 1894
页数:10
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