The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 Å resolution

Anastassios C. Papageorgiou, Rossalyn D. Brehm, Demetrios D. Leonidas, Howard S. Tranter, K. Ravi Acharya

Research output: Contribution to journalArticlepeer-review

33 Citations (SciVal)


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 languageEnglish
Pages (from-to)553-569
Number of pages17
JournalJournal of Molecular Biology
Issue number4
Publication statusPublished - 26 Jul 1996


  • Major histocompatibility complex
  • Superantigens
  • T-cell receptor
  • Toxic shock syndrome
  • X-ray crystallography

ASJC Scopus subject areas

  • Molecular Biology


Dive into the research topics of 'The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 Å resolution'. Together they form a unique fingerprint.

Cite this