Steinbacher, Stefan and Miller, Stefan and Baxa, Ulrich and Budisa, Nediljko and Weintraub, Andrej and Seckler, Robert and Huber, Robert (1997) Phage P22 tailspike protein: Crystal structure of the head-binding domain at 2.3 angstrom, fully refined structure of the endorhamnosidase at 1.56 angstrom resolution, and the molecular basis of O-antigen recognition and cleavage. JOURNAL OF MOLECULAR BIOLOGY, 267 (4). pp. 865-880. ISSN 0022-2836, 1089-8638
Full text not available from this repository.Abstract
The tailspike protein of Salmonella phage P22 is a viral adhesion protein with both receptor binding and destroying activities. It recognises the O-antigenic repeating units of cell surface lipopolysaccharide of serogroup A, B and D1 as receptor, but also inactivates its receptor by endoglycosidase (endorhamnosidase) activity. In the final step of bacteriophage P22 assembly six homotrimeric tailspike molecules are non-covalently attached to the DNA injection apparatus, mediated by their N-terminal, head-binding domains. We report the crystal structure of the head-binding domain of P22 tailspike protein at 2.3 Angstrom resolution, solved with a recombinant telluromethionine derivative and non-crystallographic symmetry averaging. The trimeric dome-like structure is formed by two perpendicular beta-sheets of five and three strands, respectively in each subunit and caps a three-helix bundle observed in the structure of the C-terminal receptor binding and cleaving fragment, reported here after full refinement at 1.56 Angstrom resolution. In the central part of the receptor binding fragment, three parallel beta-helices of 13 complete turns are associated side-by-side, while the three polypeptide strands merge into a single domain towards their C termini, with close interdigitation at the junction to the beta-helix part. Complex structures with receptor fragments from S. typhimurium, S. enteritidis and S. typhi253Ty determined at 1.8 Angstrom resolution are described in detail. Insertions into the beta-helix form the O-antigen binding groove, which also harbours the active site residues Asp392, Asp395 and Glu359. In the intact structure of the tailspike protein, head-binding and receptor-binding parts are probably linked by a flexible hinge whose function may be either to deal with shearing forces on the exposed, 150 Angstrom long tailspikes or to allow them to bend during the infection process. (C) 1997 Academic Press Limited.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PARALLEL BETA-HELIX; INFLUENZA-VIRUS; SALMONELLA-TYPHIMURIUM; PECTATE LYASE; TAIL PROTEIN; LIPOPOLYSACCHARIDE; BACTERIOPHAGE-P22; NEURAMINIDASE; HETEROGENEITY; GLYCOPROTEIN; virus protein; protein-carbohydrate recognition; endoglycosidase; telluromethionine; beta-helix |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 10 May 2023 09:59 |
| Last Modified: | 10 May 2023 09:59 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50884 |
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