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| | ==Structure of Fap-NRa at pH 5.0== | | ==Structure of Fap-NRa at pH 5.0== |
| - | <StructureSection load='3rgu' size='340' side='right' caption='[[3rgu]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='3rgu' size='340' side='right'caption='[[3rgu]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rgu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_15912 Atcc 15912]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RGU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rgu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_15912 Atcc 15912]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RGU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kub|2kub]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2kub|2kub]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fap1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1318 ATCC 15912])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fap1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1318 ATCC 15912])</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=3rgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgu OCA], [http://pdbe.org/3rgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rgu RCSB], [http://www.ebi.ac.uk/pdbsum/3rgu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rgu ProSAT]</span></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=3rgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgu OCA], [https://pdbe.org/3rgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rgu RCSB], [https://www.ebi.ac.uk/pdbsum/3rgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rgu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [[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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Atcc 15912]] | | [[Category: Atcc 15912]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Garnett, J A]] | | [[Category: Garnett, J A]] |
| | [[Category: Matthews, S J]] | | [[Category: Matthews, S J]] |
| 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 fimbriae-associated protein 1 (Fap1) is a major adhesin of Streptococcus parasanguinis, a primary colonizer of the oral cavity that plays an important role in the formation of dental plaque. Fap1 is an extracellular adhesive surface fibre belonging to the serine-rich repeat protein (SRRP) family, which plays a central role in the pathogenesis of streptococci and staphylococci. The N-terminal adhesive region of Fap1 (Fap1-NR) is composed of two domains (Fap1-NR(alpha) and Fap1-NR(beta)) and is projected away from the bacterial surface via the extensive serine-rich repeat region, for adhesion to the salivary pellicle. The adhesive properties of Fap1 are modulated through a pH switch in which a reduction in pH results in a rearrangement between the Fap1-NR(alpha) and Fap1-NR(beta) domains, which assists in the survival of S. parasanguinis in acidic environments. We have solved the structure of Fap1-NR(alpha) at pH 5.0 at 3.0A resolution and reveal how subtle rearrangements of the 3-helix bundle combined with a change in electrostatic potential mediates 'opening' and activation of the adhesive region. Further, we show that pH-dependent changes are critical for biofilm formation and present an atomic model for the inter-Fap1-NR interactions which have been assigned an important role in the biofilm formation.
Structural insight into the role of Streptococcus parasanguinis Fap1 within oral biofilm formation.,Garnett JA, Simpson PJ, Taylor J, Benjamin SV, Tagliaferri C, Cota E, Chen YY, Wu H, Matthews S Biochem Biophys Res Commun. 2012 Jan 6;417(1):421-6. Epub 2011 Dec 7. PMID:22166217[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
- ↑ Garnett JA, Simpson PJ, Taylor J, Benjamin SV, Tagliaferri C, Cota E, Chen YY, Wu H, Matthews S. Structural insight into the role of Streptococcus parasanguinis Fap1 within oral biofilm formation. Biochem Biophys Res Commun. 2012 Jan 6;417(1):421-6. Epub 2011 Dec 7. PMID:22166217 doi:10.1016/j.bbrc.2011.11.131
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