STEINBACHER, S and SECKLER, R and MILLER, S and STEIPE, B and HUBER, R and REINEMER, P (1994) CRYSTAL-STRUCTURE OF P22 TAILSPIKE PROTEIN - INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER. SCIENCE, 265 (5170). pp. 383-386. ISSN 0036-8075,
Full text not available from this repository.Abstract
The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen. It has served as a model system for genetic and biochemical analysis of protein folding. The x-ray structure of a shortened TSP (residues 109 to 666) was determined to a 2.0 angstrom resolution. Each subunit of the homotrimer contains a large parallel beta helix. The interdigitation of the polypeptide chains at the carboxyl termini is important to protrimer formation in the folding pathway and to thermostability of the mature protein.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TAIL SPIKE PROTEIN; SENSITIVE FOLDING MUTATIONS; MOLECULAR-PROPERTIES; GLOBAL SUPPRESSORS; MUTANT PROTEINS; PHAGE-P22; BACTERIOPHAGE-P22; ENDORHAMNOSIDASE; PATHWAY; INVITRO; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:40 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53198 |
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