The crystal structure of staphylococcal enterotoxin type D reveals Zn super(2+)-mediated homodimerization

Bacterial superantigens, including the staphylococcal enterotoxins, are the most potent activators of T cells known and have been suggested as a causative factor in Gram-positive shock in humans. Staphylococcal enterotoxin D (SED) is dependent upon Zn super(2+) for high affinity interactions with MH...

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Veröffentlicht in:The EMBO journal 1996-12, Vol.15 (24), p.6832-6840
Hauptverfasser: Sundstroem, M, Abrahmsen, L, Antonsson, P, Mehindate, K, Mourad, W, Dohlsten, M
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container_issue 24
container_start_page 6832
container_title The EMBO journal
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creator Sundstroem, M
Abrahmsen, L
Antonsson, P
Mehindate, K
Mourad, W
Dohlsten, M
description Bacterial superantigens, including the staphylococcal enterotoxins, are the most potent activators of T cells known and have been suggested as a causative factor in Gram-positive shock in humans. Staphylococcal enterotoxin D (SED) is dependent upon Zn super(2+) for high affinity interactions with MHC class II molecules and thus SED was co-crystallized with Zn super(2+). The crystal structure of SED has been determined in two different space groups, at 2.3 and 3.0 angstrom resolution respectively. The three-dimensional structure of SED is similar to structures of other bacterial superantigens, although this study has revealed that SED has the unique capability of forming dimers in the presence of Zn super(2+). The high affinity Zn super(2+) site used in dimer formation is located on the surface of the beta -sheet in the C-terminal domain. Two bound metal ions are coordinated by residues from both molecules in the dimer interface and thus contribute directly to formation of the dimer. A second Zn super(2+) site is located on the surface close to the domain interface of the molecule. The unique feature of SED in forming a Zn super(2+)-dependent homodimer seems to facilitate novel and biologically relevant multimeric interactions with MHC class II molecules, as shown by the induction of cytokine mRNA in human monocytes when exposed to SED and SED mutants.
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subjects Staphylococcus
title The crystal structure of staphylococcal enterotoxin type D reveals Zn super(2+)-mediated homodimerization
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