1TS2

T128A MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS

1TS2 の概要

• エントリーDOI: 10.2210/pdb1ts2/pdb
• 分子名称: TOXIC SHOCK SYNDROME TOXIN-1 (2 entities in total)
• 機能のキーワード: toxin, superantigen
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Secreted: P06886
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 66221.23

構造登録者

Earhart, C.A.,Mitchell, D.T.,Murray, D.L.,Pinheiro, D.M.,Matsumura, M.,Schlievert, P.M.,Ohlendorf, D.H. (登録日: 1997-10-09, 公開日: 1998-12-16, 最終更新日: 2024-05-22)

主引用文献

Earhart, C.A.,Mitchell, D.T.,Murray, D.L.,Pinheiro, D.M.,Matsumura, M.,Schlievert, P.M.,Ohlendorf, D.H.
Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity.
Biochemistry, 37:7194-7202, 1998

PubMed Abstract: The three-dimensional structures of five mutants of toxic shock syndrome toxin-1 (TSST-1) have been determined. These mutations are in the long central alpha helix and are useful in mapping portions of TSST-1 involved in superantigenicity and lethality. The T128A, H135A, Q139K, and I140T mutations appear to reduce superantigenicity by altering the properties of the T-cell receptor interaction surface. The Q136A mutation is at a largely buried site and causes a dramatic change in the conformation of the beta7-beta9 loop which covers the back of the central alpha helix. As this mutation has the unique ability to reduce the toxin's lethality in rabbits while retaining its superantigenicity, it raises the possibility that this rear loop mediates the ability of TSST-1 to induce lethality and suggests a route for producing nonlethal toxins for therapeutic development.

PubMed: 9585531
DOI: 10.1021/bi9721896

実験手法

X-RAY DIFFRACTION (2.3 Å)