2F0C

Structure of the Receptor Binding Protein (ORF49, bbp) from lactophage tp901-1

2F0C の概要

• エントリーDOI: 10.2210/pdb2f0c/pdb
• 関連するPDBエントリー: 1ZRU 2BSD 2BSE
• 分子名称: Phage tp901-1 ORF49 (BPP), GLYCEROL (3 entities in total)
• 機能のキーワード: beta-barrel, beta prism, 3 helix parallel bundle, viral protein
• 由来する生物種: Lactococcus phage TP901-1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 61856.93

構造登録者

Cambillau, C.,Spinelli, S. (登録日: 2005-11-13, 公開日: 2006-03-28, 最終更新日: 2023-08-23)

主引用文献

Spinelli, S.,Campanacci, V.,Blangy, S.,Moineau, S.,Tegoni, M.,Cambillau, C.
Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP901-1.
J.Biol.Chem., 281:14256-14262, 2006

PubMed Abstract: Lactococcus lactis is a gram-positive bacterium widely used by the dairy industry. Several industrial L. lactis strains are sensitive to various distinct bacteriophages. Most of them belong to the Siphoviridae family and comprise several species, among which the 936 and P335 are prominent. Members of these two phage species recognize their hosts through the interaction of their receptor-binding protein (RBP) with external cell wall saccharidices of the host, the "receptors." We report here the 1.65 A resolution crystal structure of the RBP from phage TP901-1, a member of the P335 species. This RBP of 163 amino acids is a homotrimer comprising three domains: a helical N terminus, an interlaced beta-prism, and a beta-barrel, the head domain (residues 64-163), which binds a glycerol molecule. Fluorescence quenching experiments indicated that the RBP exhibits high affinity for glycerol, muramyl-dipeptide, and other saccharides in solution. The structural comparison of this RBP with that of lactococcal phage p2 RBP, a member of the 936 species (Spinelli, S., Desmyter, A., Verrips, C. T., de Haard, J. W., Moineau, S., and Cambillau, C. (2006) Nat. Struct. Mol. Biol. 13, 85-89) suggests a large extent of modularity in RBPs of lactococcal phages.

PubMed: 16549427
DOI: 10.1074/jbc.M600666200

実験手法

X-RAY DIFFRACTION (1.65 Å)