Crystal structure of the superantigen staphylococcal enterotoxin type A

E. M. Schad, I. Zaitseva, V. N. Zaitsev, M. Dohlsten, T. Kalland, P. M. Schlievert, D. H. Ohlendorf, L. A. Svensson

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177 Scopus citations

Abstract

Staphylococcal enterotoxins are prototype superantigens characterized by their ability to bind to major histocompatibility complex (MHC) class II molecules and subsequently activate a large fraction of T-lymphocytes. The crystal structure of staphylococcal enterotoxin type A (SEA), a 27 kDa monomeric protein, was determined to 1.9 Å resolution with an R-factor of 19.9% by multiple isomorphous replacement. SEA is a two domain protein composed of a β-barrel and a β-grasp motif demonstrating the same general structure as staphylococcal enterotoxins SEE and TSST-1. Unique for SEA, however, is a Zn2+ coordination site involved in MHC class II binding. Four amino acids including Ser1, His187, His225 and Asp227 were found to be involved in direct coordination of the metal ion. SEA is the first Zn2+ binding enterotoxin that has been structurally determined.

Original languageEnglish (US)
Pages (from-to)3292-3301
Number of pages10
JournalEMBO Journal
Volume14
Issue number14
DOIs
StatePublished - 1995

Keywords

  • Staphylococcal enterotoxin A
  • Structure
  • Super-antigen
  • X-ray crystallography

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    Schad, E. M., Zaitseva, I., Zaitsev, V. N., Dohlsten, M., Kalland, T., Schlievert, P. M., Ohlendorf, D. H., & Svensson, L. A. (1995). Crystal structure of the superantigen staphylococcal enterotoxin type A. EMBO Journal, 14(14), 3292-3301. https://doi.org/10.1002/j.1460-2075.1995.tb07336.x