ArticleProtein science : a publication of the Protein Society2001
Structural features of a zinc binding site in the superantigen strepococcal pyrogenic exotoxin A (SpeA1): implications for MHC class II recognition.
Article in Protein science : a publication of the Protein Society, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 33 citations in OpenAlex.
- Review
- Disease manifestations and pathogenic mechanisms of Group A Streptococcus.Clinical microbiology reviews · 2014Review
- Gram-positive bacterial superantigen outside-in signaling causes toxic shock syndrome.The FEBS journal · 2011Review
- Zinc induces dimerization of the class II major histocompatibility complex molecule that leads to cooperative binding to a superantigen.The Journal of biological chemistry · 2007Article
- Persistence of zinc-binding bacterial superantigens at the surface of antigen-presenting cells contributes to the extreme potency of these superantigens as T-cell activators.Infection and immunity · 2005Article
- Crystal structure of a dimeric form of streptococcal pyrogenic exotoxin A (SpeA1).Protein science : a publication of the Protein Society · 2004Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Streptococcal pyrogenic exotoxin A (SpeA) is produced by Streptococcus pyogenes, and has been associated with severe infections such as scarlet fever and Streptococcal Toxic Shock Syndrome (STSS). In this study, the crystal structure of SpeA1 (the product of speA allele 1) in the presence of 2.5 mM zinc was determined at 2.8 A resolution. The protein crystallizes in the orthorhombic space group P2(1)2(1)2, with four molecules in the crystallographic asymmetric unit. The final structure has a crystallographic R-factor of 21.4% for 7,031 protein atoms, 143 water molecules, and 4 zinc atoms (one zinc atom per molecule). Four protein ligands-Glu 33, Asp 77, His 106, and His 110-form a zinc binding site that is similar to the one observed in a related superantigen, staphylococcoal enterotoxin C2. Mutant toxin forms substituting Ala for each of the zinc binding residues were generated. The affinity of these mutants for zinc ion confirms the composition of this metal binding site. The implications of zinc binding to SpeA1 for MHC class II recognition are explored using a molecular modeling approach. The results indicate that, despite their common overall architecture, superantigens appear to have multiple ways of complex formation with MHC class II molecules.
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