PDBsum entry 3da0

Viral protein

PDB id: 3da0

Contents

Protein chains

132 a.a. *

Waters ×303

* Residue conservation analysis

PDB id:

3da0

Name:

Viral protein

Title:

Crystal structure of a cleaved form of a chimeric receptor binding protein from lactococcal phages subspecies tp901-1 and p2

Structure:

Cleaved chimeric receptor binding protein from bacteriophages tp901-1 and p2. Chain: a, b, c. Engineered: yes

Source:

Lactococcus phage tp901-1, lactococcus phage p2. Organism_taxid: 35345, 254252. Gene: bpp, rbp. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.65Å R-factor: 0.165 R-free: 0.201

Authors:

M.I.Siponen,S.Blangy,S.Spinelli,L.Vera,C.Cambillau,V.Campanacci

Key ref:

M.Siponen et al. (2009). Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages. J Bacteriol, 191, 3220-3225. PubMed id: 19286807

Date:

28-May-08 Release date: 09-Jun-09

Protein chains

Q71AW2  (RBP_BPLP2) -  Receptor binding protein from Lactococcus phage p2

Seq: 264 a.a.

Struc: 132 a.a.*

Protein chains

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

Seq: 163 a.a.

Struc: 132 a.a.*

* PDB and UniProt seqs differ at 90 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

J Bacteriol 191:3220-3225 (2009)

PubMed id: 19286807

Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages.

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

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.