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| - | ==PH-INDUCED MODULATION OF STREPTOCOCCUS PARASANGUINIS ADHESION BY FAP1 FIMBRIAE== | + | |
| - | <StructureSection load='2x12' size='340' side='right' caption='[[2x12]], [[Resolution|resolution]] 2.90Å' scene=''> | + | ==pH-induced modulation of Streptococcus parasanguinis adhesion by Fap1 fimbriae== |
| | + | <StructureSection load='2x12' size='340' side='right'caption='[[2x12]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x12]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_parasanguinis Streptococcus parasanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X12 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x12]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_parasanguinis Streptococcus parasanguinis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X12 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.9Å</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=2x12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x12 RCSB], [http://www.ebi.ac.uk/pdbsum/2x12 PDBsum]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2x12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x12 OCA], [https://pdbe.org/2x12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x12 RCSB], [https://www.ebi.ac.uk/pdbsum/2x12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x12 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9ZFF9_STRPA Q9ZFF9_STRPA]] The major structural element of fimbriae. Required for adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro tooth model. A Fap1-dependent increase in adherence is seen as the pH is reduced from pH 8 to pH 5.<ref>PMID:10594831</ref> <ref>PMID:9632253</ref> | + | [https://www.uniprot.org/uniprot/FAP1_STRPA FAP1_STRPA] The major structural element of fimbriae. Required for adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro tooth model. A Fap1-dependent increase in adherence is seen as the pH is reduced from pH 8 to pH 5.<ref>PMID:10594831</ref> <ref>PMID:9632253</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2x12" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Streptococcus parasanguinis]] | | [[Category: Streptococcus parasanguinis]] |
| - | [[Category: Garnett, J]] | + | [[Category: Garnett J]] |
| - | [[Category: Matthews, S]] | + | [[Category: Matthews S]] |
| - | [[Category: Murray, J W]] | + | [[Category: Murray JW]] |
| - | [[Category: Ramboarina, S]] | + | [[Category: Ramboarina S]] |
| - | [[Category: Biofilm]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Cell wall]]
| + | |
| - | [[Category: Peptidoglycan-anchor]]
| + | |
| Structural highlights
Function
FAP1_STRPA The major structural element of fimbriae. Required for adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro tooth model. A Fap1-dependent increase in adherence is seen as the pH is reduced from pH 8 to pH 5.[1] [2]
Publication Abstract from PubMed
The serine-rich repeat (SRR) family of fimbriae play important roles in the pathogenesis of streptococci and staphylococci. Despite recent attention, their finer structural details and precise adhesion mechanisms have yet to be determined. Fap1 (Fimbriae associated protein 1) is the major structural subunit of SRR fimbriae from Streptococcus parasanguinis, and plays an essential role in fimbrial biogenesis, adhesion and the early stages of dental plaque formation. Combining multidisciplinary, high resolution structural studies with biological assays we provide new structural insight into adhesion by Fap1. We propose a model in which the serine-rich repeats of Fap1 subunits form an extended structure that projects the globular N-terminal domains away from the bacterial surface for adhesion to the salivary pellicle. We also uncover a novel pH-dependent conformational change that modulates adhesion and likely plays a role in survival in acidic environments.
Structural insights into serine-rich fimbriae from gram-positive bacteria.,Ramboarina S, Garnett JA, Zhou M, Li Y, Peng Z, Taylor JD, Lee WC, Bodey A, Murray JW, Alguel Y, Bergeron J, Bardiaux B, Sawyer E, Isaacson R, Tagliaferri C, Cota E, Nilges M, Simpson P, Ruiz T, Wu H, Matthews S J Biol Chem. 2010 Jun 28. PMID:20584910[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wu H, Fives-Taylor PM. Identification of dipeptide repeats and a cell wall sorting signal in the fimbriae-associated adhesin, Fap1, of Streptococcus parasanguis. Mol Microbiol. 1999 Dec;34(5):1070-81. PMID:10594831
- ↑ Wu H, Mintz KP, Ladha M, Fives-Taylor PM. Isolation and characterization of Fap1, a fimbriae-associated adhesin of Streptococcus parasanguis FW213. Mol Microbiol. 1998 May;28(3):487-500. PMID:9632253
- ↑ Ramboarina S, Garnett JA, Zhou M, Li Y, Peng Z, Taylor JD, Lee WC, Bodey A, Murray JW, Alguel Y, Bergeron J, Bardiaux B, Sawyer E, Isaacson R, Tagliaferri C, Cota E, Nilges M, Simpson P, Ruiz T, Wu H, Matthews S. Structural insights into serine-rich fimbriae from gram-positive bacteria. J Biol Chem. 2010 Jun 28. PMID:20584910 doi:10.1074/jbc.M110.128165
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