 |
PDBsum entry 1tyx
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral adhesion protein
|
PDB id
|
|
|
|
1tyx
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of phage p22 tailspike protein complexed with salmonella sp. O-Antigen receptors.
|
|
|
Authors
|
|
S.Steinbacher,
U.Baxa,
S.Miller,
A.Weintraub,
R.Seckler,
R.Huber.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 1996,
93,
10584-10588.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Interactions of phage p22 tails with their cellular receptor, Salmonella o-Antigen polysaccharide.
|
|
|
Authors
|
|
U.Baxa,
S.Steinbacher,
S.Miller,
A.Weintraub,
R.Huber,
R.Seckler.
|
|
|
Ref.
|
|
Biophys J, 1996,
71,
2040-2048.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Crystal structure of p22 tailspike protein: interdigitated subunits in a thermostable trimer.
|
|
|
Authors
|
|
S.Steinbacher,
R.Seckler,
S.Miller,
B.Steipe,
R.Huber,
P.Reinemer.
|
|
|
Ref.
|
|
Science, 1994,
265,
383-386.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
