3SHS

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

3SHS の概要

• エントリーDOI: 10.2210/pdb3shs/pdb
• 分子名称: Hoc head outer capsid protein, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: immunoglobulin-like domain, phage capsid decorative protein, interaction with bacteria, bacterial surface, e.coli surface, virus surface, bacteriophage surface, viral protein
• 由来する生物種: Enterobacteria phage RB49
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33389.93

構造登録者

Fokine, A.,Islam, M.Z.,Zhang, Z.,Bowman, V.D.,Rao, V.B.,Rossmann, M.G. (登録日: 2011-06-16, 公開日: 2011-06-29, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.951 Å)