2gom
From Proteopedia
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- | [[ | + | ==Crystal structure of Efb-C from Staphylococcus aureus== |
+ | <StructureSection load='2gom' size='340' side='right' caption='[[2gom]], [[Resolution|resolution]] 1.25Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2gom]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_mu50 Staphylococcus aureus subsp. aureus mu50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GOM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GOM FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gox|2gox]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">efb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 Staphylococcus aureus subsp. aureus Mu50])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gom OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gom RCSB], [http://www.ebi.ac.uk/pdbsum/2gom PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/FIB_STAAU FIB_STAAU]] Binds to host fibrinogen. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | To provide insight into bacterial suppression of complement-mediated immunity, we present here structures of a bacterial complement inhibitory protein, both free and bound to its complement target. The 1.25-A structure of the complement component C3-inhibitory domain of Staphylococcus aureus extracellular fibrinogen-binding protein (Efb-C) demonstrated a helical motif involved in complement regulation, whereas the 2.2-A structure of Efb-C bound to the C3d domain of human C3 allowed insight into the recognition of complement proteins by invading pathogens. Our structure-function studies provided evidence for a previously unrecognized mode of complement inhibition whereby Efb-C binds to native C3 and alters the solution conformation of C3 in a way that renders it unable to participate in successful 'downstream' activation of the complement response. | ||
- | + | A structural basis for complement inhibition by Staphylococcus aureus.,Hammel M, Sfyroera G, Ricklin D, Magotti P, Lambris JD, Geisbrecht BV Nat Immunol. 2007 Apr;8(4):430-7. Epub 2007 Mar 11. PMID:17351618<ref>PMID:17351618</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
- | + | ==See Also== | |
- | + | *[[Fibrinogen binding protein|Fibrinogen binding protein]] | |
- | == | + | == References == |
- | [[ | + | <references/> |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
- | < | + | [[Category: Staphylococcus aureus subsp. aureus mu50]] |
- | [[Category: Staphylococcus aureus]] | + | [[Category: Geisbrecht, B V]] |
- | [[Category: Geisbrecht, B V | + | [[Category: Hammel, M]] |
- | [[Category: Hammel, M | + | |
[[Category: Cell adhesion-toxin complex]] | [[Category: Cell adhesion-toxin complex]] | ||
[[Category: Three-helix closed bundle with left-hand twist]] | [[Category: Three-helix closed bundle with left-hand twist]] |
Revision as of 14:59, 25 December 2014
Crystal structure of Efb-C from Staphylococcus aureus
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