2F0C

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

Summary for 2F0C

• Entry DOI: 10.2210/pdb2f0c/pdb
• Related: 1ZRU 2BSD 2BSE
• Descriptor: Phage tp901-1 ORF49 (BPP), GLYCEROL (3 entities in total)
• Functional Keywords: beta-barrel, beta prism, 3 helix parallel bundle, viral protein
• Biological source: Lactococcus phage TP901-1
• Total number of polymer chains: 3
• Total formula weight: 61856.93

Authors

Cambillau, C.,Spinelli, S. (deposition date: 2005-11-13, release date: 2006-03-28, Last modification date: 2023-08-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.65 Å)