Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany.
Science. 1994 Jul 15;265(5170):383-6. doi: 10.1126/science.8023158.
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.
鼠伤寒沙门氏菌噬菌体P22的尾刺蛋白（TSP）是噬菌体附着于细菌宿主并水解O抗原的装置的一部分。它已成为蛋白质折叠遗传和生化分析的模型系统。一个缩短的TSP（残基109至666）的X射线结构被确定为2.0埃分辨率。同三聚体的每个亚基都包含一个大的平行β螺旋。多肽链在羧基末端的相互交错对于折叠途径中前三聚体的形成以及成熟蛋白的热稳定性很重要。
