2QIL
TOXIC SHOCK SYNDROME TOXIN-1 AT 2.07 A RESOLUTION
Summary for 2QIL
Entry DOI | 10.2210/pdb2qil/pdb |
Descriptor | TOXIC SHOCK SYNDROME TOXIN-1 (2 entities in total) |
Functional Keywords | staphylococcal enterotoxin, superantigen, toxic shock syndrome toxin |
Biological source | Staphylococcus aureus |
Cellular location | Secreted: P06886 |
Total number of polymer chains | 3 |
Total formula weight | 66311.31 |
Authors | Acharya, K.R.,Papageorgiou, A.C. (deposition date: 1997-03-27, release date: 1997-08-12, Last modification date: 2024-02-21) |
Primary citation | Papageorgiou, A.C.,Brehm, R.D.,Leonidas, D.D.,Tranter, H.S.,Acharya, K.R. The refined crystal structure of toxic shock syndrome toxin-1 at 2.07 A resolution. J.Mol.Biol., 260:553-569, 1996 Cited by PubMed Abstract: The pyrogenic toxin toxic shock syndrome toxin-1 from Staphylococcus aureus is a causative agent of the toxic shock syndrome disease. It belongs to a family of proteins known as superantigens that cross-link major histocompatibility class II molecules and T-cell receptors leading to the activation of a substantial number of T cells. The crystal structure of this protein has been refined to 2.07 A with an Rcryst value of 20.4% for 51,240 reflections. The final model contains three molecules in the asymmetric unit with good stereochemistry and a root-mean-square deviation of 0.009 A and 1.63 from ideality for bond lengths and bond angles, respectively. The overall fold is considerably similar to that of other known microbial superantigens (staphylococcal enterotoxins). However, a detailed structural analysis shows that toxic shock syndrome toxin-1 lacks several structural features that affect its specificity for V beta elements of the T-cell receptor and also its recognition by major histocompatibility class II molecules. PubMed: 8759320DOI: 10.1006/jmbi.1996.0421 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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