1M4V

Crystal structure of SET3, a superantigen-like protein from Staphylococcus aureus

Summary for 1M4V

• Entry DOI: 10.2210/pdb1m4v/pdb
• Descriptor: SET3, superantigen-like protein (2 entities in total)
• Functional Keywords: ob-fold, beta-grasp, superantigen fold, immune system
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 48429.68

Authors

Arcus, V.L.,Langley, R.,Proft, T.,Fraser, J.D.,Baker, E.N. (deposition date: 2002-07-05, release date: 2002-07-17, Last modification date: 2024-02-14)

Primary citation

Arcus, V.L.,Langley, R.,Proft, T.,Fraser, J.D.,Baker, E.N.
The three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome
J.Biol.Chem., 277:32274-32281, 2002

PubMed Abstract: The staphylococcal enterotoxin-like toxins (SETs) are a family of proteins encoded within the Staphylococcus aureus genome that were identified by their similarity to the well described bacterial superantigens. The first crystal structure of a member of the SET family, SET3, has been determined to 1.9 A (R = 0.205, R(free) = 0.240) and reveals a fold characteristic of the superantigen family but with significant differences. The SET proteins are secreted at varying levels by staphylococcal isolates, and seroconversion studies of normal individuals indicate that they are strongly antigenic to humans. Recombinant SETs do not exhibit any of the properties expected of superantigens such as major histocompatibility complex class II binding or broad T-cell activation, suggesting they have an entirely different function. The fact that the whole gene family is clustered within the pathogenicity island SaIn2 of the S. aureus genome suggests that they are involved in host/pathogen interactions.

PubMed: 12082105
DOI: 10.1074/jbc.M203914200

Experimental method

X-RAY DIFFRACTION (1.9 Å)