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

被引：277

作者：

STEINBACHER, S ^{[1
]}

SECKLER, R ^{[1
]}

MILLER, S ^{[1
]}

STEIPE, B ^{[1
]}

HUBER, R ^{[1
]}

REINEMER, P ^{[1
]}

机构：

[1] UNIV REGENSBURG,D-93040 REGENSBURG,GERMANY

来源：

SCIENCE | 1994年 / 265卷 / 5170期

关键词：

D O I：

10.1126/science.8023158

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：383 / 386

页数：4

共 34 条

[1] 3-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS-AERUGINOSA - A 2-DOMAIN PROTEIN WITH A CALCIUM-BINDING PARALLEL-BETA ROLL MOTIF [J].