1ZRU
structure of the lactophage p2 receptor binding protein in complex with glycerol
1ZRU の概要
エントリーDOI | 10.2210/pdb1zru/pdb |
関連するPDBエントリー | 2BSD 2BSE |
分子名称 | lactophage p2 receptor binding protein, GLYCEROL (3 entities in total) |
機能のキーワード | 3 domains: beta barrel, beta prism, beta barrel, structural genomics, structural proteomics in europe, spine, viral protein |
由来する生物種 | Lactococcus lactis phage p2 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 86556.74 |
構造登録者 | Spinelli, S.,Tremblay, D.M.,Tegoni, M.,Blangy, S.,Huyghe, C.,Desmyter, A.,Labrie, S.,de Haard, H.,Moineau, S.,Cambillau, C.,Structural Proteomics in Europe (SPINE) (登録日: 2005-05-22, 公開日: 2006-03-28, 最終更新日: 2023-08-23) |
主引用文献 | Tremblay, D.M.,Tegoni, M.,Spinelli, S.,Campanacci, V.,Blangy, S.,Huyghe, C.,Desmyter, A.,Labrie, S.,Moineau, S.,Cambillau, C. Receptor-binding protein of Lactococcus lactis phages: identification and characterization of the saccharide receptor-binding site. J.Bacteriol., 188:2400-2410, 2006 Cited by PubMed Abstract: Phage p2, a member of the lactococcal 936 phage species, infects Lactococcus lactis strains by binding initially to specific carbohydrate receptors using its receptor-binding protein (RBP). The structures of p2 RBP, a homotrimeric protein composed of three domains, and of its complex with a neutralizing llama VH domain (VHH5) have been determined (S. Spinelli, A. Desmyter, C. T. Verrips, H. J. de Haard, S. Moineau, and C. Cambillau, Nat. Struct. Mol. Biol. 13:85-89, 2006). Here, we show that VHH5 was able to neutralize 12 of 50 lactococcal phages belonging to the 936 species. Moreover, escape phage mutants no longer neutralized by VHH5 were isolated from 11 of these phages. All of the mutations (but one) cluster in the RBP/VHH5 interaction surface that delineates the receptor-binding area. A glycerol molecule, observed in the 1.7-A resolution structure of RBP, was found to bind tightly (Kd= 0.26 microM) in a crevice located in this area. Other saccharides bind RBP with comparable high affinity. These data prove the saccharidic nature of the bacterial receptor recognized by phage p2 and identify the position of its binding site in the RBP head domain. PubMed: 16547026DOI: 10.1128/JB.188.7.2400-2410.2006 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.73 Å) |
構造検証レポート
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