1TSP

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

Summary for 1TSP

• Entry DOI: 10.2210/pdb1tsp/pdb
• Descriptor: TAILSPIKE-PROTEIN (2 entities in total)
• Functional Keywords: late protein
• Biological source: Enterobacteria phage P22
• Cellular location: Virion (Potential): P12528
• Total number of polymer chains: 1
• Total formula weight: 60265.27

Authors

Steinbacher, S.,Seckler, R.,Miller, S.,Steipe, B.,Huber, R.,Reinemer, P. (deposition date: 1994-06-16, release date: 1995-09-15, Last modification date: 2024-02-14)

Primary citation

Steinbacher, S.,Seckler, R.,Miller, S.,Steipe, B.,Huber, R.,Reinemer, P.
Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.
Science, 265:383-386, 1994

PubMed 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.

PubMed: 8023158

Experimental method

X-RAY DIFFRACTION (2 Å)