Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.
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.
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany.
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Steinbacher
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Seckler
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Miller
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Steipe
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Huber
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P
Reinemer
D017100:Bacteriophage P22; D003196:Computer Graphics; D003460:Crystallization; D018360:Crystallography, X-Ray; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D017354:Point Mutation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics; D017376:Viral Tail Proteins
D014764:Viral Proteins; D017376:Viral Tail Proteins; D006026:Glycoside Hydrolases; C083268:tailspike protein, bacteriophage