1YN3

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

Summary for 1YN3

• Entry DOI: 10.2210/pdb1yn3/pdb
• Descriptor: truncated cell surface protein map-w (2 entities in total)
• Functional Keywords: virulence-factor, toxin, extracellular-adherence protein, staphylococcus, protein binding
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 21620.37

Authors

Geisbrecht, B.V.,Hamaoka, B.Y.,Perman, B.,Zemla, A.,Leahy, D.J. (deposition date: 2005-01-23, release date: 2005-03-01, Last modification date: 2023-08-23)

Primary citation

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.
J.Biol.Chem., 280:17243-17250, 2005

PubMed Abstract: 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.

PubMed: 15691839
DOI: 10.1074/jbc.M412311200

Experimental method

X-RAY DIFFRACTION (1.35 Å)