乳酸乳球菌噬菌体bIL170受体结合蛋白头部结构域的晶体结构
Crystal structure of the receptor-binding protein head domain from Lactococcus lactis phage bIL170.
作者信息
Ricagno Stefano, Campanacci Valérie, Blangy Stéphanie, Spinelli Silvia, Tremblay Denise, Moineau Sylvain, Tegoni Mariella, Cambillau Christian
机构信息
Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités Aix-Marseille I & II, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
出版信息
J Virol. 2006 Sep;80(18):9331-5. doi: 10.1128/JVI.01160-06.
Abstract
Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry, is subject to lytic phage infections. In the first step of infection, phages recognize the host saccharidic receptor using their receptor binding protein (RBP). Here, we report the 2.30-A-resolution crystal structure of the RBP head domain from phage bIL170. The structure of the head monomer is remarkably close to those of other lactococcal phages, p2 and TP901-1, despite any sequence identity with them. The knowledge of the three-dimensional structures of three RBPs gives a better insight into the module exchanges which have occurred among phages.
摘要
乳酸乳球菌是一种被乳制品行业广泛使用的革兰氏阳性细菌，容易受到裂解性噬菌体的感染。在感染的第一步，噬菌体利用其受体结合蛋白（RBP）识别宿主糖类受体。在此，我们报道了噬菌体bIL170的RBP头部结构域的2.30埃分辨率晶体结构。尽管与其他乳酸球菌噬菌体p2和TP901-1没有序列同一性，但头部单体的结构与它们的结构非常相似。三种RBP的三维结构知识有助于更好地了解噬菌体之间发生的模块交换。
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本文引用的文献
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Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP901-1.乳酸乳球菌噬菌体受体结合蛋白的模块化结构。温和噬菌体TP901-1的RBP结构。
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Receptor-binding protein of Lactococcus lactis phages: identification and characterization of the saccharide receptor-binding site.乳酸乳球菌噬菌体的受体结合蛋白：糖类受体结合位点的鉴定与表征
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