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

Steinbacher S; Seckler R; Miller S; Steipe B; Huber R; Reinemer P

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

Science 265: 383-6 (1994)

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.

Mesh Headings

Bacteriophage P22*

Computer Graphics

Crystallization

Crystallography, X-Ray

Glycoside Hydrolases*

Models, Molecular

Point Mutation

Protein Conformation

Protein Folding*

Protein Structure, Secondary

Protein Structure, Tertiary*

Support, Non-U.S. Gov't

Viral Proteins*

Unique Identifier: 94294807

Chemical Identifiers (Names)

EC 3.2.1. (Glycoside Hydrolases)

EC 3.2.1.- (bacteriophage P22 tailspike protein)

(Viral Proteins)