3D8M

Crystal structure of a chimeric receptor binding protein from lactococcal phages subspecies TP901-1 and p2

3D8M の概要

• エントリーDOI: 10.2210/pdb3d8m/pdb
• 関連するPDBエントリー: 1ZRU 2BSD 2BSE 2F0C
• 分子名称: Baseplate protein, Receptor binding protein (1 entity in total)
• 機能のキーワード: lactococcal phage p2, lactococcal phage tp901-1, receptor binding protein, virus-viral protein complex, virus/viral protein
• 由来する生物種: Lactococcus phage TP901-1; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17872.09

構造登録者

Siponen, M.I.,Blangy, S.,Spinelli, S.,Cambillau, C.,Campanacci, V. (登録日: 2008-05-23, 公開日: 2009-04-14, 最終更新日: 2023-11-01)

主引用文献

Siponen, M.,Spinelli, S.,Blangy, S.,Moineau, S.,Cambillau, C.,Campanacci, V.
Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages
J.Bacteriol., 191:3220-3225, 2009

PubMed Abstract: Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry to manufacture cheeses, is subject to infection by a diverse population of virulent phages. We have previously determined the structures of three receptor binding proteins (RBPs) from lactococcal phages TP901-1, p2, and bIL170, each of them having a distinct host range. Virulent phages p2 and bIL170 are classified within the 936 group, while the temperate phage TP901-1 is a member of the genetically distinct P335 polythetic group. These RBPs comprise three domains: the N-terminal domain, binding to the virion particle; a beta-helical linker domain; and the C-terminal domain, bearing the receptor binding site used for host recognition. Here, we have designed, expressed, and determined the structure of an RBP chimera in which the N-terminal and linker RBP domains of phage TP901-1 (P335) are fused to the C-terminal RBP domain of phage p2 (936). This chimera exhibits a stable structure that closely resembles the parental structures, while a slight displacement of the linker made RBP domain adaptation efficient. The receptor binding site is structurally indistinguishable from that of native p2 RBP and binds glycerol with excellent affinity.

PubMed: 19286807
DOI: 10.1128/JB.01637-08

実験手法

X-RAY DIFFRACTION (3.35 Å)