1ste
From Proteopedia
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|PDB= 1ste |SIZE=350|CAPTION= <scene name='initialview01'>1ste</scene>, resolution 2.0Å | |PDB= 1ste |SIZE=350|CAPTION= <scene name='initialview01'>1ste</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ste FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ste OCA], [http://www.ebi.ac.uk/pdbsum/1ste PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ste RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Acharya, K R.]] | [[Category: Acharya, K R.]] | ||
[[Category: Papageorgiou, A C.]] | [[Category: Papageorgiou, A C.]] | ||
| - | [[Category: ZN]] | ||
[[Category: enterotoxin]] | [[Category: enterotoxin]] | ||
[[Category: superantigen]] | [[Category: superantigen]] | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:42 2008'' |
Revision as of 20:46, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STAPHYLOCOCCAL ENTEROTOXIN C2 FROM STAPHYLOCOCCUS AUREUS
Overview
BACKGROUND: 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. RESULTS: The crystal structure of SEC2 has been determined at 2.0 A resolution. The overall topology of the molecule resembles that of SEB and TSST-1, and the regions corresponding to the MHC class II and T-cell receptor binding sites on SEB are quite similar in SEC2. A unique feature of SEC2 is the presence of a zinc ion located in a solvent-exposed region at the interface between the two domains of the molecule. The zinc ion is coordinated to Asp83, His118, His122 and Asp9* (from the neighbouring molecule in the crystal lattice). Atomic absorption spectrometry demonstrates that zinc is also bound to SEC2 in solution. CONCLUSIONS: SEC2 appears to be capable of binding to MHC class II molecules in much the same manner as SEB. However, structure-function studies have suggested an alternative binding mode that involves a different site on the toxin. The zinc ion of SEC2 lies within this region and thus may be important for complex formation, for example by acting as a bridge between the two molecules. Other possible roles for the metal cation, including a catalytic one, are also considered.
About this Structure
1STE is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site., Papageorgiou AC, Acharya KR, Shapiro R, Passalacqua EF, Brehm RD, Tranter HS, Structure. 1995 Aug 15;3(8):769-79. PMID:7582894
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