2x12

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[[Image:2x12.png|left|200px]]
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==PH-INDUCED MODULATION OF STREPTOCOCCUS PARASANGUINIS ADHESION BY FAP1 FIMBRIAE==
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<StructureSection load='2x12' size='340' side='right' caption='[[2x12]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2x12| PDB=2x12 | SCENE= }}
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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>
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===PH-INDUCED MODULATION OF STREPTOCOCCUS PARASANGUINIS ADHESION BY FAP1 FIMBRIAE===
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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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{{ABSTRACT_PUBMED_20584910}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:020584910</ref><references group="xtra"/>
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[[Category: Streptococcus parasanguinis]]
[[Category: Streptococcus parasanguinis]]
[[Category: Garnett, J.]]
[[Category: Garnett, J.]]

Revision as of 13:23, 22 October 2014

PH-INDUCED MODULATION OF STREPTOCOCCUS PARASANGUINIS ADHESION BY FAP1 FIMBRIAE

2x12, resolution 2.90Å

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