2x12

pH-induced modulation of Streptococcus parasanguinis adhesion by Fap1 fimbriae

spinqualitylabelsall models 2x12, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: MSE 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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