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Science 15 July 1994:
Vol. 265. no. 5170, pp. 383 - 386
DOI: 10.1126/science.8023158
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Articles

Science, Vol 265, Issue 5170, 383-386
Copyright © 1994 by American Association for the Advancement of Science

articles

Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer

S Steinbacher, R Seckler, S Miller, B Steipe, R Huber, and P Reinemer

Max-Planck-Institut fur Biochemie, Abteilung Strukturforschung, Martinsried, Germany.

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.


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