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| | <StructureSection load='1r19' size='340' side='right'caption='[[1r19]], [[Resolution|resolution]] 3.51Å' scene=''> | | <StructureSection load='1r19' size='340' side='right'caption='[[1r19]], [[Resolution|resolution]] 3.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r19]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"albococcus_epidermidis"_winslow_and_winslow_1908 "albococcus epidermidis" winslow and winslow 1908]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R19 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R19 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r19]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R19 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;'>[[1r17|1r17]]</div></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]] 3.51Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sdrG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1282 "Albococcus epidermidis" Winslow and Winslow 1908])</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=1r19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r19 OCA], [https://pdbe.org/1r19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r19 RCSB], [https://www.ebi.ac.uk/pdbsum/1r19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r19 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r19 OCA], [http://pdbe.org/1r19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r19 RCSB], [http://www.ebi.ac.uk/pdbsum/1r19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r19 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SDRG_STAEP SDRG_STAEP]] Binds to the N-terminus of the B beta-chain of human fibrinogen and thereby interferes with thrombin cleavage and release of fibrinopeptide B, thus interfering with fibrin clot formation. This may hinder host defense against microbial infections.<ref>PMID:11371571</ref> | + | [https://www.uniprot.org/uniprot/SDRG_STAEP SDRG_STAEP] Binds to the N-terminus of the B beta-chain of human fibrinogen and thereby interferes with thrombin cleavage and release of fibrinopeptide B, thus interfering with fibrin clot formation. This may hinder host defense against microbial infections.<ref>PMID:11371571</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Albococcus epidermidis winslow and winslow 1908]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bowden, M G]] | + | [[Category: Staphylococcus epidermidis]] |
| - | [[Category: Choe, D]] | + | [[Category: Bowden MG]] |
| - | [[Category: Davis, S]] | + | [[Category: Choe D]] |
| - | [[Category: Gurusiddappa, S]] | + | [[Category: Davis S]] |
| - | [[Category: Hook, M]] | + | [[Category: Gurusiddappa S]] |
| - | [[Category: Moore, D]] | + | [[Category: Hook M]] |
| - | [[Category: Narayana, S V.L]] | + | [[Category: Moore D]] |
| - | [[Category: Ponnuraj, K]] | + | [[Category: Narayana SVL]] |
| - | [[Category: Xu, Y]] | + | [[Category: Ponnuraj K]] |
| - | [[Category: Cell adhesion]]
| + | [[Category: Xu Y]] |
| - | [[Category: Mscramm]]
| + | |
| - | [[Category: Sdrg native]]
| + | |
| Structural highlights
Function
SDRG_STAEP Binds to the N-terminus of the B beta-chain of human fibrinogen and thereby interferes with thrombin cleavage and release of fibrinopeptide B, thus interfering with fibrin clot formation. This may hinder host defense against microbial infections.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Gram-positive pathogens such as staphylococci contain multiple cell wall-anchored proteins that serve as an interface between the microbe and its environment. Some of these proteins act as adhesins and mediate bacterial attachment to host tissues. SdrG is a cell wall-anchored adhesin from Staphylococcus epidermidis that binds to the Bbeta chain of human fibrinogen (Fg) and is necessary and sufficient for bacterial attachment to Fg-coated biomaterials. Here, we present the crystal structures of the ligand binding region of SdrG as an apoprotein and in complex with a synthetic peptide analogous to its binding site in Fg. Analysis of the crystal structures, along with mutational studies of both the protein and of the peptide, reveals that SdrG binds to its ligand with a dynamic "dock, lock, and latch" mechanism. We propose that this mechanism represents a general mode of ligand binding for structurally related cell wall-anchored proteins of gram-positive bacteria.
A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen.,Ponnuraj K, Bowden MG, Davis S, Gurusiddappa S, Moore D, Choe D, Xu Y, Hook M, Narayana SV Cell. 2003 Oct 17;115(2):217-28. PMID:14567919[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Davis SL, Gurusiddappa S, McCrea KW, Perkins S, Hook M. SdrG, a fibrinogen-binding bacterial adhesin of the microbial surface components recognizing adhesive matrix molecules subfamily from Staphylococcus epidermidis, targets the thrombin cleavage site in the Bbeta chain. J Biol Chem. 2001 Jul 27;276(30):27799-805. Epub 2001 May 22. PMID:11371571 doi:http://dx.doi.org/10.1074/jbc.M103873200
- ↑ Ponnuraj K, Bowden MG, Davis S, Gurusiddappa S, Moore D, Choe D, Xu Y, Hook M, Narayana SV. A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen. Cell. 2003 Oct 17;115(2):217-28. PMID:14567919
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