1tsp
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(New page: 200px<br /><applet load="1tsp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tsp, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 01:26, 21 November 2007
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CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER
Overview
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.
About this Structure
1TSP is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer., Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P, Science. 1994 Jul 15;265(5170):383-6. PMID:8023158
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