2x12

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(Difference between revisions)

Revision as of 16:47, 3 November 2021

pH-induced modulation of Streptococcus parasanguinis adhesion by Fap1 fimbriae

Structural highlights

2x12 is a 2 chain structure with sequence from Atcc 15912. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x12"

@@ Line 3: / Line 3: @@
 <StructureSection load='2x12' size='340' side='right'caption='[[2x12]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x12]] is a 2 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=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/Atcc_15912 Atcc 15912]. 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>
-<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://pdbe.org/2x12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x12 RCSB], [http://www.ebi.ac.uk/pdbsum/2x12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x12 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=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>
 == 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;">
 == Publication Abstract from PubMed ==

2x12

From Proteopedia

Revision as of 16:47, 3 November 2021

pH-induced modulation of Streptococcus parasanguinis adhesion by Fap1 fimbriae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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