Crystal Structure of P22 Tailspike Protein: Interdigitated Subunits in a Thermostable Trimer
- 15 July 1994
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 265 (5170) , 383-386
- https://doi.org/10.1126/science.8023158
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.Keywords
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