This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2gom

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:28, 14 February 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of Efb-C from Staphylococcus aureus==
==Crystal structure of Efb-C from Staphylococcus aureus==
-
<StructureSection load='2gom' size='340' side='right' caption='[[2gom]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
+
<StructureSection load='2gom' size='340' side='right'caption='[[2gom]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2gom]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. 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>
+
<table><tr><td colspan='2'>[[2gom]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</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 STAAM])</td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gom OCA], [https://pdbe.org/2gom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gom RCSB], [https://www.ebi.ac.uk/pdbsum/2gom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gom ProSAT]</span></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://pdbe.org/2gom PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gom RCSB], [http://www.ebi.ac.uk/pdbsum/2gom PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gom ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/FIB_STAAU FIB_STAAU]] Binds to host fibrinogen.
+
[https://www.uniprot.org/uniprot/FIB_STAAM FIB_STAAM] Binds to host fibrinogen (By similarity).
-
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 2gom" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Fibrinogen binding protein|Fibrinogen binding protein]]
*[[Fibrinogen binding protein|Fibrinogen binding protein]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Staam]]
+
[[Category: Large Structures]]
-
[[Category: Geisbrecht, B V]]
+
[[Category: Staphylococcus aureus subsp. aureus Mu50]]
-
[[Category: Hammel, M]]
+
[[Category: Geisbrecht BV]]
-
[[Category: Cell adhesion-toxin complex]]
+
[[Category: Hammel M]]
-
[[Category: Three-helix closed bundle with left-hand twist]]
+

Current revision

Crystal structure of Efb-C from Staphylococcus aureus

PDB ID 2gom

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools