1TYX

TITLE OF TAILSPIKE-PROTEIN

Summary for 1TYX

• Entry DOI: 10.2210/pdb1tyx/pdb
• Descriptor: TAILSPIKE PROTEIN, alpha-D-galactopyranose-(1-2)-[alpha-D-Abequopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose-(1-3)-alpha-D-galactopyranose-(1-2)-[alpha-D-Abequopyranose-(1-3)]alpha-D-mannopyranose-(1-4)-alpha-L-rhamnopyranose (3 entities in total)
• Functional Keywords: complex, viral adhesion protein, receptor, endoglycosidase carbohydrate, cell receptor, recognition, binding protein lipopolysaccharide
• Biological source: Enterobacteria phage P22
• Cellular location: Virion (Potential): P12528
• Total number of polymer chains: 1
• Total formula weight: 60835.79

Authors

Steinbacher, S.,Huber, R. (deposition date: 1996-07-26, release date: 1997-07-23, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)