1tsp: Difference between revisions

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{{STRUCTURE_1tsp|  PDB=1tsp  |  SCENE=  }}  
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'''CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER'''
===CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER===




==Overview==
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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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{{ABSTRACT_PUBMED_8023158}}


==About this Structure==
==About this Structure==
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[[Category: Steipe, B.]]
[[Category: Steipe, B.]]
[[Category: Late protein]]
[[Category: Late protein]]
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Revision as of 01:18, 29 July 2008

File:1tsp.png

Template:STRUCTURE 1tsp

CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER

Template:ABSTRACT PUBMED 8023158

About this Structure

1TSP is a Single protein structure of sequence from Enterobacteria phage p22. 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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