2gom: Difference between revisions

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<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 [https://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 [https://proteopedia.org/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"><div style='overflow: auto; max-height: 3em;'>[[2gox|2gox]]</div></td></tr>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">efb ([https://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>
</table>
</table>
== Function ==
== Function ==
[[https://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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Staam]]
[[Category: Staphylococcus aureus subsp. aureus Mu50]]
[[Category: Geisbrecht, B V]]
[[Category: Geisbrecht BV]]
[[Category: Hammel, M]]
[[Category: Hammel M]]
[[Category: Cell adhesion-toxin complex]]
[[Category: Three-helix closed bundle with left-hand twist]]

Revision as of 13:38, 14 December 2022

Crystal structure of Efb-C from Staphylococcus aureusCrystal structure of Efb-C from Staphylococcus aureus

Structural highlights

2gom is a 2 chain structure with sequence from Staphylococcus aureus subsp. aureus Mu50. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FIB_STAAM Binds to host fibrinogen (By similarity).

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Hammel M, Sfyroera G, Ricklin D, Magotti P, Lambris JD, Geisbrecht BV. A structural basis for complement inhibition by Staphylococcus aureus. Nat Immunol. 2007 Apr;8(4):430-7. Epub 2007 Mar 11. PMID:17351618 doi:10.1038/ni1450

2gom, resolution 1.25Å

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