View source for 2kub


==Solution structure of the alpha subdomain of the major non-repeat unit of Fap1 fimbriae of Streptococcus parasanguis==
<StructureSection load='2kub' size='340' side='right'caption='[[2kub]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kub]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_parasanguinis Streptococcus parasanguinis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KUB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kub OCA], [https://pdbe.org/2kub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kub RCSB], [https://www.ebi.ac.uk/pdbsum/2kub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kub ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== 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<ref>PMID:20584910</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kub" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus parasanguinis]]
[[Category: Bardiaux B]]
[[Category: Bodey A]]
[[Category: Garnett JA]]
[[Category: Matthews S]]
[[Category: Nilges M]]
[[Category: Ramboarina S]]
[[Category: Simpson P]]