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

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(?). Here, Fap1-NR(?) 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.

SUBMITTER: Garnett JA

PROVIDER: S-EPMC3034626 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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

Garnett James A JA Ramboarina Stéphanie S Lee Wei-chao WC Tagliaferri Camille C Wu Wilfred W Matthews Stephen S

Acta crystallographica. Section F, Structural biology and crystallization communications 20110127 Pt 2

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 ...[more]

PMID: 21301104

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