Crystal structure and location of gp131 in the bacteriophage phiKZ virion
Crystal structure and location of gp131 in the bacteriophage phiKZ virion
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DOI：
10.1016/j.virol.2012.09.001
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发表时间：
2012-12-20
期刊：
影响因子：
3.7
通讯作者：
Leiman, Petr G.
中科院分区：
文献类型：
--
作者：
Sycheva, Lada V.;Shneider, Mikhail M.;Leiman, Petr G.
假单胞菌噬菌体Phi KZ和它的两个近亲Phi PA3和201 Phi 2-1是非常大的噬菌体，由于它们的基因组与GenBank的其他序列数据非常不同，它们在噬菌体分类中形成了一个独立的分支。Phi KZ的收缩尾巴由至少32种不同的蛋白质组成，但只有一种确定的结构功能被分配给其中一种-尾鞘蛋白。在这里，我们报告了另一种phiKZ尾蛋白基因产物131(Gp131C)的C-末端结构域的晶体结构。我们发现gp131位于基板的外围，并且可能与基板发出的纤维相关联。Gp131C是一种七叶贝塔螺旋桨，其形状为倾斜的环状。Gp131C表面的一个小但高度保守的带负电荷的斑块对于底物结合或与不同的尾蛋白相互作用可能是重要的。(C)2012 Elsevier Inc.保留所有权利。
Pseudomonas phage phi KZ and its two close relatives phi PA3 and 201 phi 2-1 are very large bacteriophages that form a separate branch in phage classification because their genomes are very different from the rest of GenBank sequence data. The contractile tail of phi KZ is built from at least 32 different proteins, but a definitive structural function is assigned to only one of them-the tail sheath protein. Here, we report the crystal structure of the C-terminal domain of another phiKZ tail protein, gene product 131 (gp131C). We show that gp131 is located at the periphery of the baseplate and possibly associates with fibers that emanate from the baseplate. Gp131C is a seven-bladed beta-propeller that has a shape of a skewed toroid. A small but highly conserved and negatively charged patch on the surface of gp131C might be important for substrate binding or for interaction with a different tail protein. (C) 2012 Elsevier Inc. All rights reserved.