PDBsum entry 2bsd

Receptor

PDB id: 2bsd

Contents

Protein chains

254 a.a. *

Waters ×215

* Residue conservation analysis

PDB id:

2bsd

Name:

Receptor

Title:

Structure of lactococcal bacteriophage p2 receptor binding protein

Structure:

Receptor binding protein. Chain: a, b, c. Engineered: yes

Source:

Enterobacteria phage p2. Organism_taxid: 10679. Strain: lm0230. Expressed in: escherichia coli k-12. Expression_system_taxid: 83333

Biol. unit:

Trimer (from PDB file)

Resolution:

2.30Å R-factor: 0.221 R-free: 0.252

Authors:

S.Spinelli,A.Desmyter,C.T.Verrips,H.J.W.Dehaard,S.Moineau,C.Cambillau

Key ref:

S.Spinelli et al. (2006). Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat Struct Mol Biol, 13, 85-89. PubMed id: 16327804 DOI: 10.1038/nsmb1029

Date:

20-May-05 Release date: 02-Nov-05

Protein chains

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

Seq: 264 a.a.

Struc: 254 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nsmb1029

Nat Struct Mol Biol 13:85-89 (2006)

PubMed id: 16327804

Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses.

S.Spinelli, A.Desmyter, C.T.Verrips, H.J.de Haard, S.Moineau, C.Cambillau.

ABSTRACT

Lactococcus lactis is a Gram-positive bacterium used extensively by the dairy industry for the manufacture of fermented milk products. The double-stranded DNA bacteriophage p2 infects specific L. lactis strains using a receptor-binding protein (RBP) located at the tip of its noncontractile tail. We have solved the crystal structure of phage p2 RBP, a homotrimeric protein composed of three domains: the shoulders, a beta-sandwich attached to the phage; the neck, an interlaced beta-prism; and the receptor-recognition head, a seven-stranded beta-barrel. We used the complex of RBP with a neutralizing llama VHH domain to identify the receptor-binding site. Structural similarity between the recognition-head domain of phage p2 and those of adenoviruses and reoviruses, which invade mammalian cells, suggests that these viruses, despite evolutionary distant targets, lack of sequence similarity and the different chemical nature of their genomes (DNA versus RNA), might have a common ancestral gene.

Selected figure(s)

Figure 2.
Figure 2. Individual domains of the receptor-binding protein from phage p2. (a) The shoulder domain, with a rainbow color gradient from the N-terminus (blue) to the C-terminus (red). -strands are numbered sequentially 1-8. Dashed line indicates the absence of residues 10-18 in the electron density map. (b) The neck -prism domain formed by the interlaced assembly of three segments within positions 142-163. The three faces of the -prism are identified by the letters A, B and C; the strands in each subunit are numbered 1-4. (c) The head domain with a rainbow color gradient from the N-terminus (blue) to the C-terminus (red). -strands are numbered sequentially 1-7. The view is rotated 90° from that in b. (d) Common double Greek-key topology shared by phage p2, adenovirus and reovirus RBPs. The fourth strand of the Greek-key motif is disordered in phage p2. (e) Sequence alignment of the RBPs from phages p2, sk1 and bIL170. The secondary structure of phage p2 RBP is indicated above the alignments and -strands are colored red, green or blue to denote their location in the shoulders, neck or head, respectively (alignment made by MULTALIN (http://prodes.toulouse.inra.fr/multalin/multalin.html)).

Figure 3.
Figure 3. The complex of the phage p2 RBP head with VHH5. (a) The RBP-VHH5 complex. The three head domains, the only parts of RBP observed in the structure of the complex, are in gray. The three VHH5s are colored red, green and blue. (b) Views of the surface of the RBP-head trimer that interacts with VHH5 (white). Inset, spheres representation of the RBP-head residues interacting with VHH5. Residues labeled with and without asterisks are from different monomers. (c) VHH5 CDR1 (red), CDR2 (green) and CDR3 (blue). The surface interacting with the RBP is circled by a white line encompassing part of the CDRs.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2006, 13, 85-89) copyright 2006.

Figures were selected by an automated process.