1UNS
IDENTIFICATION OF A SECONDARY ZINC-BINDING SITE IN STAPHYLOCOCCAL ENTEROTOXIN C2: IMPLICATIONS FOR SUPERANTIGEN RECOGNITION
Summary for 1UNS
Entry DOI | 10.2210/pdb1uns/pdb |
Related | 1CQV 1I4P 1I4Q 1I4R 1I4X 1SE2 1STE |
Descriptor | ENTEROTOXIN TYPE C-2, ZINC ION (3 entities in total) |
Functional Keywords | superantigen, toxin, enterotoxin, zinc-binding site |
Biological source | STAPHYLOCOCCUS AUREUS |
Cellular location | Secreted: P34071 |
Total number of polymer chains | 1 |
Total formula weight | 27753.78 |
Authors | Papageorgiou, A.C.,Baker, M.D.,McLeod, J.D.,Goda, S.,Sansom, D.M.,Tranter, H.S.,Acharya, K.R. (deposition date: 2003-09-15, release date: 2003-11-13, Last modification date: 2024-11-06) |
Primary citation | Papageorgiou, A.C.,Baker, M.D.,Mcleod, J.D.,Goda, S.,Manzotti, C.N.,Sanson, D.M.,Tranter, H.S.,Acharya, K.R. Identification of a Secondary Zinc-Binding Site in Staphylococcal Enterotoxin C2: Implications for Superantigen Recognition J.Biol.Chem., 279:1297-, 2004 Cited by PubMed Abstract: The previously determined crystal structure of the superantigen staphylococcal enterotoxin C2 (SEC2) showed binding of a single zinc ion located between the N- and C-terminal domains. Here we present the crystal structure of SEC2 determined to 2.0 A resolution in the presence of additional zinc. The structure revealed the presence of a secondary zinc-binding site close to the major histocompatibility complex (MHC)-binding site of the toxin and some 28 A away from the primary zinc-binding site of the toxin found in previous studies. T cell stimulation assays showed that varying the concentration of zinc ions present affected the activity of the toxin and we observed that high zinc concentrations considerably inhibited T cell responses. This indicates that SEC2 may have multiple modes of interaction with the immune system that are dependent on serum zinc levels. The potential role of the secondary zinc-binding site and that of the primary one in the formation of the TCR.SEC2.MHC complex are considered, and the possibility that zinc may regulate the activity of SEC2 as a toxin facilitating different T cell responses is discussed. PubMed: 14559915DOI: 10.1074/JBC.M307333200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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