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| ==Crystal structure of the collagen binding domain of Erysipelothrix rhusiopathiae surface protein RspB== | | ==Crystal structure of the collagen binding domain of Erysipelothrix rhusiopathiae surface protein RspB== |
| <StructureSection load='3v10' size='340' side='right' caption='[[3v10]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='3v10' size='340' side='right'caption='[[3v10]], [[Resolution|resolution]] 1.75Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3v10]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_insidiosus"_trevisan_1885 "bacillus insidiosus" trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V10 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V10 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3v10]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erysipelothrix_rhusiopathiae Erysipelothrix rhusiopathiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V10 FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z1p|2z1p]], [[2f6a|2f6a]]</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]] 1.75Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rspB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1648 "Bacillus insidiosus" Trevisan 1885])</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=3v10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v10 OCA], [https://pdbe.org/3v10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v10 RCSB], [https://www.ebi.ac.uk/pdbsum/3v10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v10 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=3v10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v10 OCA], [http://pdbe.org/3v10 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v10 RCSB], [http://www.ebi.ac.uk/pdbsum/3v10 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v10 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q83VG5_ERYRH Q83VG5_ERYRH] |
| BACKGROUND: Pathogenic bacteria specifically recognize extracellular matrix (ECM) molecules of the host (e.g. collagen, fibrinogen and fibronectin) through their surface proteins known as MSCRAMMs (Microbial Surface Components Recognizing Adhesive Matrix Molecules) and initiate colonization. On implantation, biomaterials easily get coated with these ECM molecules and the MSCRAMMs mediate bacterial adherence to biomaterials. With the rapid rise in antibiotic resistance, designing alternative strategies to reduce/eliminate bacterial colonization is absolutely essential. METHODS: The Rhusiopathiae surface protein B (RspB) is a collagen-binding MSCRAMM of Erysipelothrix rhusiopathiae. It also binds to abiotic surfaces. The crystal structure of the collagen-binding region of RspB (rRspB31-348) reported here revealed that RspB also binds collagen by a unique ligand binding mechanism called "Collagen Hug" which is a common theme for collagen-binding MSCRAMMs of many Gram-positive bacteria. Here, we report the interaction studies between rRspB31-348 and silver nanoparticles using methods like gel shift assay, gel permeation chromatography and circular dichroism spectroscopy. RESULTS: The "Collagen Hug" mechanism was inhibited in the presence of silver nanoparticles as rRspB31-348 was unable to bind to collagen. The total loss of binding was likely because of rRspB31-348 and silver nanoparticle protein corona formation and not due to the loss of the structural integrity of rRspB31-348 on binding with nanoparticles as observed from circular dichroism experiments. GENERAL SIGNIFICANCE: Interaction of rRspB31-348 with silver nanoparticle impaired its ligand binding mechanism. Details of this inhibition mechanism may be useful for the development of antimicrobial materials and antiadhesion drugs.
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| Collagen adhesin-nanoparticle interaction impairs adhesin's ligand binding mechanism.,Devi AS, Ogawa Y, Shimoji Y, Balakumar S, Ponnuraj K Biochim Biophys Acta. 2012 Jul;1820(7):819-28. doi: 10.1016/j.bbagen.2012.04.006., Epub 2012 Apr 17. PMID:22538248<ref>PMID:22538248</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3v10" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus insidiosus trevisan 1885]] | | [[Category: Erysipelothrix rhusiopathiae]] |
| [[Category: Ogawa, Y]] | | [[Category: Large Structures]] |
| [[Category: Ponnuraj, K]] | | [[Category: Ogawa Y]] |
| [[Category: Shimoji, Y]] | | [[Category: Ponnuraj K]] |
| [[Category: Subramainan, B]] | | [[Category: Shimoji Y]] |
| [[Category: Devi, A Swarmistha]] | | [[Category: Subramainan B]] |
| [[Category: Cell adhesion]]
| | [[Category: Swarmistha devi A]] |
| [[Category: Collagen binding protein]]
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| [[Category: Collagen hug model]]
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| [[Category: Dev-igg fold]]
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| [[Category: Rhusiopathiae surface protein b]]
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