Steinbacher, Stefan and Baxa, Ulrich and Miller, Stefan and Weintraub, Andrej and Seckler, Robert and Huber, Robert (1996) Crystal structure of phage P22 tailspike protein complexed with Salmonella sp O-antigen receptors. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 93 (20). pp. 10584-10588. ISSN 0027-8424, 1091-6490
Full text not available from this repository.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 typhiumurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined at 1.8 Angstrom 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PARALLEL BETA-HELIX; INFLUENZA-VIRUS; SIALIC-ACID; LIPOPOLYSACCHARIDE; HETEROGENEITY; NEURAMINIDASE; RECOGNITION; ANTIBODY; TYPHIMURIUM; MECHANISMS; endoglycosidase; hemagglutinin; neuraminidase; virus; infection |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 22 Jun 2023 10:11 |
| Last Modified: | 22 Jun 2023 10:11 |
| URI: | https://pred.uni-regensburg.de/id/eprint/51455 |
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