PDBsum entry 2f0c

Viral protein

PDB id: 2f0c

Contents

Protein chains

147 a.a. *

Ligands

GOL ×3

Waters ×715

* Residue conservation analysis

PDB id:

2f0c

Name:

Viral protein

Title:

Structure of the receptor binding protein (orf49, bbp) from lactophage tp901-1

Structure:

Phage tp901-1 orf49 (bpp). Chain: a, b, c. Engineered: yes

Source:

Lactococcus phage tp901-1. Organism_taxid: 35345. Gene: orf49/bbp. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Biol. unit:

Trimer (from PQS)

Resolution:

1.65Å R-factor: 0.158 R-free: 0.189

Authors:

C.Cambillau,S.Spinelli

Key ref:

S.Spinelli et al. (2006). 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. PubMed id: 16549427

Date:

13-Nov-05 Release date: 28-Mar-06

Protein chains

Q9G096  (Q9G096_9CAUD) -  BPP from Lactococcus phage TP901-1

Seq: 163 a.a.

Struc: 147 a.a.

Enzyme reactions

• Enzyme class: E.C.?

J Biol Chem 281:14256-14262 (2006)

PubMed id: 16549427

Modular structure of the receptor binding proteins of Lactococcus lactis phages. The RBP structure of the temperate phage TP901-1.

S.Spinelli, V.Campanacci, S.Blangy, S.Moineau, M.Tegoni, C.Cambillau.

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.