PDBsum entry 3shs

Viral protein

PDB id: 3shs

Contents

Protein chain

303 a.a.

Metals

_MG

Waters ×90

PDB id:

3shs

Name:

Viral protein

Title:

Three n-terminal domains of the bacteriophage rb49 highly immunogenic outer capsid protein (hoc)

Structure:

Hoc head outer capsid protein. Chain: a. Fragment: 3 n-terminal immunoglobulin domains (unp residues 1-304). Engineered: yes

Source:

Enterobacteria phage rb49. Organism_taxid: 50948. Gene: hoc. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.95Å R-factor: 0.223 R-free: 0.267

Authors:

A.Fokine,M.Z.Islam,Z.Zhang,V.D.Bowman,V.B.Rao,M.G.Rossmann

Key ref:

A.Fokine et al. (2011). Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage. J Virol, 85, 8141-8148. PubMed id: 21632759

Date:

16-Jun-11 Release date: 29-Jun-11

Protein chain

Q7Y442  (Q7Y442_BPRB4) -  Hoc head outer capsid protein from Escherichia phage RB49

Seq: 404 a.a.

Struc: 303 a.a.

Enzyme reactions

• Enzyme class: E.C.?

J Virol 85:8141-8148 (2011)

PubMed id: 21632759

Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage.

A.Fokine, M.Z.Islam, Z.Zhang, V.D.Bowman, V.B.Rao, M.G.Rossmann.

ABSTRACT

The head of bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein (Hoc). One Hoc molecule binds near the center of each hexameric capsomer. Hoc is dispensable for capsid assembly and has been used to display pathogenic antigens on the surface of T4. Here we report the crystal structure of a protein containing the first three of four domains of Hoc from bacteriophage RB49, a close relative of T4. The structure shows an approximately linear arrangement of the protein domains. Each of these domains has an immunoglobulin-like fold, frequently found in cell attachment molecules. In addition, we report biochemical data suggesting that Hoc can bind to Escherichia coli, supporting the hypothesis that Hoc could attach the phage capsids to bacterial surfaces and perhaps also to other organisms. The capacity for such reversible adhesion probably provides survival advantages to the bacteriophage.