The Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens

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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 {angstrom} 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 ... continued below

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Geisbrecht, B V; Hamaoka, B Y; Perman, B; Zemla, A & Leahy, D J October 14, 2005.

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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 {angstrom} 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.

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PDF-file: 18 pages; size: 0 Kbytes

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  • Journal Name: The Journal of Biological Chemistry; Journal Volume: 280; Journal Issue: 17

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  • Report No.: UCRL-JRNL-216376
  • Grant Number: W-7405-ENG-48
  • Office of Scientific & Technical Information Report Number: 885398
  • Archival Resource Key: ark:/67531/metadc892488

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Reports, articles and other documents harvested from the Office of Scientific and Technical Information.

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  • October 14, 2005

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  • Sept. 23, 2016, 2:42 p.m.

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  • Nov. 23, 2016, 12:08 p.m.

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Geisbrecht, B V; Hamaoka, B Y; Perman, B; Zemla, A & Leahy, D J. The Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens, article, October 14, 2005; Livermore, California. (digital.library.unt.edu/ark:/67531/metadc892488/: accessed October 18, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.