Structural Conservation of the Myoviridae Phage Tail Sheath Protein Fold
Structural Conservation of the Myoviridae Phage Tail Sheath Protein Fold
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DOI：
10.1016/j.str.2011.09.012
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发表时间：
2011-12-07
期刊：
影响因子：
5.7
通讯作者：
Rossmann, Michael G.
中科院分区：
文献类型：
--
作者：
Aksyuk, Anastasia A.;Kurochkina, Lidia P.;Rossmann, Michael G.
噬菌体phiKZ是一种巨大的噬菌体，感染人类病原体铜绿假单胞菌。phiKZ病毒粒子由直径为1450埃的二十面体头部和2000埃长的可收缩尾部组成。整个病毒的结构以前曾有报道，表明其在伸展状态下的尾部组织与充分研究的Myovirus噬菌体T4尾部相似。phiKZ尾鞘蛋白片段的晶体结构被确定为2.4埃分辨率。此外，两个原噬菌体尾鞘蛋白的晶体结构被确定为1.9和3.3埃分辨率。尽管这些蛋白质之间的序列同一性较低，但所有这些结构都具有相似的折叠。phiKZ尾鞘蛋白的晶体结构已被安装到低温电子显微镜重建的延长尾鞘和多鞘。发现phiKZ尾鞘收缩的结构重排与噬菌体T4的结构重排相似。
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.