1m4v
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(New page: 200px<br /><applet load="1m4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m4v, resolution 1.90Å" /> '''Crystal structure of...)
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Revision as of 01:38, 25 November 2007
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Crystal structure of SET3, a superantigen-like protein from Staphylococcus aureus
Overview
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.
About this Structure
1M4V is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
The Three-dimensional structure of a superantigen-like protein, SET3, from a pathogenicity island of the Staphylococcus aureus genome., Arcus VL, Langley R, Proft T, Fraser JD, Baker EN, J Biol Chem. 2002 Aug 30;277(35):32274-81. Epub 2002 Jun 24. PMID:12082105
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