ArticleProtein science : a publication of the Protein Society2004
Crystal structure of a dimeric form of streptococcal pyrogenic exotoxin A (SpeA1).
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 17 citations in OpenAlex.
- Proinflammatory synergy between protease and superantigen streptococcal pyogenic exotoxins.Infection and immunity · 2025Article
- Disulfide bond formation in prokaryotes.Nature microbiology · 2018Review
- Zinc'ing it out: zinc homeostasis mechanisms and their impact on the pathogenesis of human pathogen group A streptococcus.Metallomics : integrated biometal science · 2017Review
- The contribution of group A streptococcal virulence determinants to the pathogenesis of sepsis.Virulence · 2014Review
- Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii.The Journal of biological chemistry · 2013Article
- Gram-positive bacterial superantigen outside-in signaling causes toxic shock syndrome.The FEBS journal · 2011Review
- Mutagenesis, biochemical, and biophysical characterization of Mycoplasma arthritidis-derived mitogen.Molecular immunology · 2007Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
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Abstract
Streptococcal pyrogenic exotoxin A (SpeA1) is a bacterial superantigen associated with scarlet fever and streptococcal toxic shock syndrome (STSS). SpeA1 is found in both monomeric and dimeric forms, and previous work suggested that the dimer results from an intermolecular disulfide bond between the cysteines at positions 90 of each monomer. Here, we present the crystal structure of the dimeric form of SpeA1. The toxin crystallizes in the orthorhombic space group P212121, with two dimers in the crystallographic asymmetric unit. The final structure has a crystallographic R-factor of 21.52% for 7248 protein atoms, 136 water molecules, and 4 zinc atoms (one zinc atom per molecule). The implications of SpeA1 dimer on MHC class II and T-cell receptor recognition are discussed.
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