2gom: Difference between revisions
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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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