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首页> 外文期刊>Journal of Molecular Biology >PHAGE P22 TAILSPIKE PROTEIN - CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN AT 2.3 ANGSTROM, FULLY REFINED STRUCTURE OF THE ENDORHAMNOSIDASE AT 1.56 ANGSTROM RESOLUTION, AND THE MOLECULAR BASIS OF O-ANTIGEN RECOGNITION AND CLEAVAGE
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PHAGE P22 TAILSPIKE PROTEIN - CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN AT 2.3 ANGSTROM, FULLY REFINED STRUCTURE OF THE ENDORHAMNOSIDASE AT 1.56 ANGSTROM RESOLUTION, AND THE MOLECULAR BASIS OF O-ANTIGEN RECOGNITION AND CLEAVAGE

机译：噬菌体蛋白P22阶段-头结合域在2.3埃时的晶体结构，内啡肽酶的精细结构在1.56埃时的解析度以及O-抗原识别和裂解的分子基础

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摘要

The tailspike protein of Salmonella phage P22 is a viral adhesion protein with both receptor binding and destroying activities. It recognises the O-antigenic repeating units of cell surface lipopolysaccharide of serogroup A, B and D1 as receptor, but also inactivates its receptor by endoglycosidase (endorhamnosidase) activity. In the final step of bacteriophage P22 assembly six homotrimeric tailspike molecules are non-covalently attached to the DNA injection apparatus, mediated by their N-terminal, head-binding domains. We report the crystal structure of the head-binding domain of P22 tailspike protein at 2.3 Angstrom resolution, solved with a recombinant telluromethionine derivative and non-crystallographic symmetry averaging. The trimeric dome-like structure is formed by two perpendicular beta-sheets of five and three strands, respectively in each subunit and caps a three-helix bundle observed in the structure of the C-terminal receptor binding and cleaving fragment, reported here after full refinement at 1.56 Angstrom resolution. In the central part of the receptor binding fragment, three parallel beta-helices of 13 complete turns are associated side-by-side, while the three polypeptide strands merge into a single domain towards their C termini, with close interdigitation at the junction to the beta-helix part. Complex structures with receptor fragments from S. typhimurium, S. enteritidis and S. typhi253Ty determined at 1.8 Angstrom resolution are described in detail. Insertions into the beta-helix form the O-antigen binding groove, which also harbours the active site residues Asp392, Asp395 and Glu359. In the intact structure of the tailspike protein, head-binding and receptor-binding parts are probably linked by a flexible hinge whose function may be either to deal with shearing forces on the exposed, 150 Angstrom long tailspikes or to allow them to bend during the infection process. (C) 1997 Academic Press Limited. [References: 69]
机译：沙门氏菌噬菌体P22的尾钉蛋白是一种病毒粘附蛋白，具有受体结合和破坏活性。它识别血清型A，B和D1的细胞表面脂多糖的O抗原重复单元为受体，但也通过糖苷内切酶（内啡肽酶）活性使其受体失活。在噬菌体P22组装的最后步骤中，六个同三聚体尾钉分子非共价连接至DNA注射装置，由它们的N末端，头部结合结构域介导。我们报告了2.3埃分辨率的P22尾钉蛋白的头部结合域的晶体结构，用重组碲甲硫氨酸衍生物和平均结晶对称性解决。三聚体的圆顶状结构由分别在每个亚基中的五个和三个链的两个垂直β-折叠形成，并覆盖了在C端受体结合和裂解片段的结构中观察到的三螺旋束，在完整报道后在此报道分辨率为1.56埃。在受体结合片段的中心部分，三个完整的13个完整匝的平行β螺旋并排相连，而这三个多肽链则向其C末端融合成单个结构域，在与C末端的连接处紧密交指。 β-螺旋部分。详细描述了带有鼠伤寒沙门氏菌，肠炎沙门氏菌和鼠伤寒沙门氏菌253Ty受体片段的复杂结构，分辨率为1.8埃。插入β-螺旋形成O-抗原结合槽，该槽还包含活性位点残基Asp392，Asp395和Glu359。在尾钉蛋白的完整结构中，头部结合和受体结合部分可能通过柔性铰链连接，该铰链的功能可能是处理暴露在外的150埃长的尾钉上的剪切力，或者使其在弯曲过程中弯曲。感染过程。 （C）1997 Academic Press Limited。 [参考：69]

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