1TSP

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

1TSP の概要

• エントリーDOI: 10.2210/pdb1tsp/pdb
• 分子名称: TAILSPIKE-PROTEIN (2 entities in total)
• 機能のキーワード: late protein
• 由来する生物種: Enterobacteria phage P22
• 細胞内の位置: Virion (Potential): P12528
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60265.27

構造登録者

Steinbacher, S.,Seckler, R.,Miller, S.,Steipe, B.,Huber, R.,Reinemer, P. (登録日: 1994-06-16, 公開日: 1995-09-15, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)