Literature DB >> 21301104

Crystallization and initial crystallographic analysis of the Streptococcus parasanguinis FW213 Fap1-NRα adhesive domain at pH 5.0.

James A Garnett1, Stéphanie Ramboarina, Wei-chao Lee, Camille Tagliaferri, Wilfred Wu, Stephen Matthews.   

Abstract

The adhesin fimbriae-associated protein 1 (Fap1) is a surface protein of Streptococcus parasanguinis FW213 and plays a major role in the formation of dental plaque in humans. Increased adherence is highly correlated to a reduction in pH and acid activation has been mapped to a subdomain: Fap1-NR(α). Here, Fap1-NR(α) has been crystallized at pH 5.0 and diffraction data have been collected to 3.0 Å resolution. The crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 122.0, c = 117.8 Å. It was not possible to conclusively determine the number of molecules in the asymmetric unit and heavy-atom derivatives are now being prepared.

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Year:  2011        PMID: 21301104      PMCID: PMC3034626          DOI: 10.1107/S1744309110052772

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  13 in total

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4.  Isolation and characterization of Fap1, a fimbriae-associated adhesin of Streptococcus parasanguis FW213.

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5.  The Fap1 fimbrial adhesin is a glycoprotein: antibodies specific for the glycan moiety block the adhesion of Streptococcus parasanguis in an in vitro tooth model.

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Journal:  Mol Microbiol       Date:  2002-01       Impact factor: 3.501

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Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

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8.  A conserved C-terminal 13-amino-acid motif of Gap1 is required for Gap1 function and necessary for the biogenesis of a serine-rich glycoprotein of Streptococcus parasanguinis.

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Review 9.  The integration of macromolecular diffraction data.

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Review 10.  Scaling and assessment of data quality.

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  3 in total

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