3SHS

Three N-terminal domains of the bacteriophage RB49 Highly Immunogenic Outer Capsid protein (Hoc)

Summary for 3SHS

• Entry DOI: 10.2210/pdb3shs/pdb
• Descriptor: Hoc head outer capsid protein, MAGNESIUM ION (3 entities in total)
• Functional Keywords: immunoglobulin-like domain, phage capsid decorative protein, interaction with bacteria, bacterial surface, e.coli surface, virus surface, bacteriophage surface, viral protein
• Biological source: Enterobacteria phage RB49
• Total number of polymer chains: 1
• Total formula weight: 33389.93

Authors

Fokine, A.,Islam, M.Z.,Zhang, Z.,Bowman, V.D.,Rao, V.B.,Rossmann, M.G. (deposition date: 2011-06-16, release date: 2011-06-29, Last modification date: 2024-02-28)

Primary citation

Fokine, A.,Islam, M.Z.,Zhang, Z.,Bowman, V.D.,Rao, V.B.,Rossmann, M.G.
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, 2011

PubMed 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.

PubMed: 21632759
DOI: 10.1128/JVI.00847-11

Experimental method

X-RAY DIFFRACTION (1.951 Å)