1yn4
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(New page: 200px<br /><applet load="1yn4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yn4, resolution 1.80Å" /> '''Crystal Structures o...)
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Revision as of 02:15, 25 November 2007
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Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens
Overview
The Eap (extracellular adherence protein) of Staphylococcus aureus, functions as a secreted virulence factor by mediating interactions between, the bacterial cell surface and several extracellular host proteins. Eap, proteins from different Staphylococcal strains consist of four to six, tandem repeats of a structurally uncharacterized domain (EAP domain). We, have determined the three-dimensional structures of three different EAP, domains to 1.8, 2.2, and 1.35 A resolution, respectively. These structures, reveal a core fold that is comprised of an alpha-helix lying diagonally, across a five-stranded, mixed beta-sheet. Comparison of EAP domains with, known structures reveals an unexpected homology with the C-terminal domain, of bacterial superantigens. Examination of the structure of the, superantigen SEC2 bound to the beta-chain of a T-cell receptor suggests a, possible ligand-binding site within the EAP domain (Fields, B. A., Malchiodi, E. L., Li, H., Ysern, X., Stauffacher, C. V., Schlievert, P., M., Karjalainen, K., and Mariuzza, R. (1996) Nature 384, 188-192). These, results provide the first structural characterization of EAP domains, relate EAP domains to a large class of bacterial toxins, and will guide, the design of future experiments to analyze EAP domain structure/function, relationships.
About this Structure
1YN4 is a Single protein structure of sequence from Staphylococcus aureus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structures of EAP domains from Staphylococcus aureus reveal an unexpected homology to bacterial superantigens., Geisbrecht BV, Hamaoka BY, Perman B, Zemla A, Leahy DJ, J Biol Chem. 2005 Apr 29;280(17):17243-50. Epub 2005 Feb 3. PMID:15691839
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