1yn5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1yn5.gif|left|200px]] | [[Image:1yn5.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1yn5", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
| | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| | or leave the SCENE parameter empty for the default display. | ||
--> | |||
{{STRUCTURE_1yn5| PDB=1yn5 | SCENE= }} | |||
}} | |||
'''Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens''' | '''Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens''' | ||
| Line 30: | Line 27: | ||
[[Category: Perman, B.]] | [[Category: Perman, B.]] | ||
[[Category: Zemla, A.]] | [[Category: Zemla, A.]] | ||
[[Category: | [[Category: Extracellular adherence protein]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: | [[Category: Toxin]] | ||
[[Category: | [[Category: Virulence factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:31:58 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 16:32, 3 May 2008
Crystal Structures of EAP Domains from Staphylococcus aureus Reveal an Unexpected Homology to Bacterial Superantigens
OverviewOverview
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 StructureAbout this Structure
1YN5 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 16:31:58 2008