Abstract
The pyrogenic toxin toxic shock syndrome toxin-1 from Staphylococcus aureus is a causative agent of the toxic shock syndrome disease. It belongs to a family of proteins known as superantigens that cross-link major histocompatibility class II molecules and T-cell receptors leading to the activation of a substantial number of T cells. The crystal structure of this protein has been refined to 2.07 Å with an R(cryst) value of 20.4% for 51,240 reflections. The final model contains three molecules in the asymmetric unit with good stereochemistry and a root-mean-square deviation of 0.009 Å and 1.63° from ideality for bond lengths and bond angles, respectively. The overall fold is considerably similar to that of other known microbial superantigens (staphylococcal enterotoxins). However, a detailed structural analysis shows that toxic shock syndrome toxin-1 lacks several structural features that affect its specificity for Vβ elements of the T-cell receptor and also its recognition by major histocompatibility class II molecules.
| Original language | English |
|---|---|
| Pages (from-to) | 553-569 |
| Number of pages | 17 |
| Journal | Journal of Molecular Biology |
| Volume | 260 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 26 Jul 1996 |
Funding
We thank the staff at EMBL Hamburg outstation (c/o DESY) and CLRC laboratory at Daresbury for support during data collection; David Stuart, Yvonne Jones and Karl Harlos for their initial contribution to the project; Edward Passalacqua for help in producing crystals for high resolution crystallographic work; Tony Rees and Peter Hambleton for the encouragement; Don Wiley and his colleagues for providing the atomic co-ordinates of the SEB-DR1 and TSST-DR1 complexes. This work was supported by the Medical Research Council and the Nuffield Foundation through grants to KRA.
Keywords
- Major histocompatibility complex
- Superantigens
- T-cell receptor
- Toxic shock syndrome
- X-ray crystallography
ASJC Scopus subject areas
- Molecular Biology