1STE

STAPHYLOCOCCAL ENTEROTOXIN C2 FROM STAPHYLOCOCCUS AUREUS

Summary for 1STE

• Entry DOI: 10.2210/pdb1ste/pdb
• Descriptor: STAPHYLOCOCCAL ENTEROTOXIN C2, ZINC ION (3 entities in total)
• Functional Keywords: superantigen, toxin, enterotoxin
• Biological source: Staphylococcus aureus
• Cellular location: Secreted: P34071
• Total number of polymer chains: 1
• Total formula weight: 27688.38

Authors

Acharya, K.R.,Papageorgiou, A.C. (deposition date: 1995-08-21, release date: 1996-12-23, Last modification date: 2024-10-30)

Primary citation

Papageorgiou, A.C.,Acharya, K.R.,Shapiro, R.,Passalacqua, E.F.,Brehm, R.D.,Tranter, H.S.
Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site.
Structure, 3:769-779, 1995

PubMed Abstract: Staphylococcus aureus enterotoxin C2 (SEC2) belongs to a family of proteins, termed 'superantigens', that form complexes with class II MHC molecules enabling them to activate a substantial number of T cells. Although superantigens seem to act by a common mechanism, they vary in many of their specific interactions and biological properties. Comparison of the structure of SEC2 with those of two other superantigens--staphylococcal enterotoxin B (SEB) and toxic shock syndrome toxin-1 (TSST-1)--may provide insight into their mode of action.

PubMed: 7582894
DOI: 10.1016/S0969-2126(01)00212-X

Experimental method

X-RAY DIFFRACTION (2 Å)