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3rgu

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Current revision (12:23, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3rgu' size='340' side='right'caption='[[3rgu]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3rgu' size='340' side='right'caption='[[3rgu]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[3rgu]] is a 4 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=3RGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RGU FirstGlance]. <br>
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</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>
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</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&#8491;</td></tr>
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<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>
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<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>
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<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>
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<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>
<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 ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:22166217</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rgu" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 15912]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Garnett, J A]]
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[[Category: Streptococcus parasanguinis]]
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[[Category: Matthews, S J]]
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[[Category: Garnett JA]]
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[[Category: Adhesion]]
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[[Category: Matthews SJ]]
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[[Category: Cell wall]]
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[[Category: Dental cary]]
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[[Category: Helical bundle]]
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[[Category: Peptidoglycan-anchor]]
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[[Category: Ph]]
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[[Category: Structural protein]]
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Current revision

Structure of Fap-NRa at pH 5.0

PDB ID 3rgu

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