Steinbacher, Stefan and Miller, Stefan and Baxa, Ulrich and Weintraub, Andrej and Seckler, Robert (1997) Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography. BIOLOGICAL CHEMISTRY, 378 (3-4). pp. 337-343. ISSN 1431-6730, 1437-4315
Full text not available from this repository.Abstract
The O-antigenic repeating units of the Salmonella cell surface lipopolysaccharides (serotypes A, B and D1) serve as receptors for phage P22, This initial binding step is mediated by the tailspike protein (TSP), which is present in six copies on the base plate of the phage, In addition to the binding activity, TSP also displays a low endoglycolytic activity, cleaving the alpha(1,3)-O-glycosidic bond between rhamnose and galactose of the O-antigenic repeats, The crystal structure of TSP in complex with receptor fragments allowed to identify the receptor binding site for the octasaccharide product of the enzymatic action of TSP on delipidated LPS and the active site consisting of Asp392, Asp395 and Glu359. The structure comprises a large right-handed parallel beta-helix of 13 turns. These fold independently in the trimer, whereas the N-terminus forms a cap-like structure and the C-terminal parts of the three polypeptide strands merge to a single common domain, In addition, TSP has served as model system for the folding of large, multisubunit proteins, Its folding pathway is influenced by a large number of point mutations, classified as lethal, temperature sensitive or general suppressor mutations, which influence the partitioning between aggregation and the productive folding pathway.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PARALLEL BETA-HELIX; TAIL SPIKE PROTEIN; TAILSPIKE PROTEIN; INFLUENZA-VIRUS; CRYSTAL-STRUCTURE; MUTANT PROTEINS; BINDING DOMAIN; IN-VITRO; BACTERIOPHAGE-P22; LIPOPOLYSACCHARIDE; endoglycosidase; beta-helix; phage mutants; protein folding; receptor binding; virus protein |
| 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: | 11 May 2023 10:09 |
| Last Modified: | 11 May 2023 10:09 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50984 |
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