1TYV

STRUCTURE OF TAILSPIKE-PROTEIN

1TYV の概要

• エントリーDOI: 10.2210/pdb1tyv/pdb
• 分子名称: TAILSPIKE PROTEIN (2 entities in total)
• 機能のキーワード: complex, viral adhesion protein, receptor, endoglycosidase carbohydrate, cell receptor, recognition, binding protein lipopolysaccharide
• 由来する生物種: Enterobacteria phage P22
• 細胞内の位置: Virion (Potential): P12528
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59616.65

構造登録者

Steinbacher, S.,Huber, R. (登録日: 1996-07-26, 公開日: 1997-07-23, 最終更新日: 2024-02-14)

主引用文献

Steinbacher, S.,Baxa, U.,Miller, S.,Weintraub, A.,Seckler, R.,Huber, R.
Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.
Proc.Natl.Acad.Sci.USA, 93:10584-10588, 1996

PubMed Abstract: The O-antigenic repeating units of lipopolysaccharides from Salmonella serogroups A, B, and D1 serve as receptors for the phage P22 tailspike protein, which also has receptor destroying endoglycosidase (endorhamnosidase) activity, integrating the functions of both hemagglutinin and neuraminidase in influenza virus. Crystal structures of the tailspike protein in complex with oligosaccharides, comprising two O-antigenic repeating units from Salmonella typhimurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as catalytic residues was identified. Kinetics of binding and cleavage suggest a role of the receptor destroying endorhamnosidase activity primarily for detachment of newly assembled phages.

PubMed: 8855221
DOI: 10.1073/pnas.93.20.10584

実験手法

X-RAY DIFFRACTION (1.8 Å)