1GOZ

Structural basis for the altered T-cell receptor binding specificty in a superantigenic staphylococcus aureus Enterotoxin-B mutant

Summary for 1GOZ

• Entry DOI: 10.2210/pdb1goz/pdb
• Related: 1D5M 1D5X 1D5Z 1D6E 1SBB 1SE3 1SE4 1SEB 2SEB 3SEB
• Descriptor: ENTEROTOXIN TYPE B (2 entities in total)
• Functional Keywords: enterotoxin, staphylococcal enterotoxins, seb, enterotoxin b
• Biological source: STAPHYLOCOCCUS AUREUS
• Total number of polymer chains: 2
• Total formula weight: 56794.08

Authors

Baker, M.D.,Papageorgiou, A.C.,Acharya, K.R. (deposition date: 2001-10-29, release date: 2002-02-13, Last modification date: 2024-11-13)

Primary citation

Baker, M.D.,Papageorgiou, A.C.,Titball, R.,Miller, J.,White, S.,Lingard, B.,Lee, J.,Cavanagh, D.,Kehoe, M.,Robinson, J.,Acharya, K.R.
Structural and Functional Role of Threonine 112 in a Superantigen Staphylococcus Aureus Enterotoxin B.
J.Biol.Chem., 277:2756-, 2002

PubMed Abstract: Bacterial superantigens are potent T-cell stimulatory protein molecules produced by Staphylococcus aureus and Streptococcus pyogenes. Their superantigenic activity can be attributed to their ability to cross-link major histocompatibility complex class II molecules with T-cell receptors (TCRs) to form a tri-molecular complex. Each superantigen is known to interact with a specific V(beta) element of TCR. Staphylococcal enterotoxin B (SEB, a superantigen), a primary cause of food poisoning, is also responsible for a significant percentage of non-menstrual associated toxic shock syndrome in patients with a variety of staphylococcal infections. Structural studies have elucidated a binding cavity on the toxin molecule essential for TCR binding. To understand the crucial residues involved in binding, mutagenesis analysis was performed. Our analysis suggest that mutation of a conserved residue Thr(112) to Ser (T112S) in the binding cavity induces a selective reduction in the affinity for binding one TCR V(beta) family and can be attributed to the structural differences in the native and mutant toxins. We present a detailed comparison of the mutant structure determined at 2.0 A with the previously reported native SEB and SEB-TCR V(beta) complex structures.

PubMed: 11704673
DOI: 10.1074/JBC.M109369200

Experimental method

X-RAY DIFFRACTION (2 Å)