3OWE

Crystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a High Affinity Mutant Mouse T-cell Receptor Chain

Summary for 3OWE

• Entry DOI: 10.2210/pdb3owe/pdb
• Related: 1XXG 3MC0
• Descriptor: Beta-chain, Enterotoxin SEG (3 entities in total)
• Functional Keywords: t-cell receptor v beta domain, complex structure, igg domains, b grasp, virulence factors, immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 16
• Total formula weight: 313512.39

Authors

Fernandez, M.M.,Cho, S.,Robinson, H.,Mariuzza, R.A.,Malchiodi, M.L. (deposition date: 2010-09-17, release date: 2010-11-03, Last modification date: 2024-10-16)

Primary citation

Fernandez, M.M.,Cho, S.,De Marzi, M.C.,Kerzic, M.C.,Robinson, H.,Mariuzza, R.A.,Malchiodi, E.L.
Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor {beta} chain.
J.Biol.Chem., 286:1189-1195, 2011

PubMed Abstract: Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR β chain (mVβ8.2) and staphylococcal enterotoxin G (SEG) at 2.0 Å resolution revealed a binding site that does not conserve the "hot spots" present in mVβ8.2-SEC2, mVβ8.2-SEC3, mVβ8.2-SEB, and mVβ8.2-SPEA complexes. Analysis of the mVβ8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mVβ8.2 by SEG. This mode of interaction between SEG and mVβ8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host.

PubMed: 21059660
DOI: 10.1074/jbc.M110.142471

Experimental method

X-RAY DIFFRACTION (2.6 Å)