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The pilin protein FimP from Actinomyces oris: crystal structure and sequence analyses
Umeå University, Faculty of Science and Technology, Department of Chemistry. (Karina Persson)
Umeå University, Faculty of Medicine, Department of Odontology, Cariology.
Umeå University, Faculty of Medicine, Department of Odontology, Cariology.
Umeå University, Faculty of Medicine, Department of Odontology, Cariology.
2012 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 7, no 10, e48364- p.Article in journal (Refereed) Published
Abstract [en]

The Actinomyces oris type-1 pili are important for the initial formation of dental plaque by binding to salivary proteins that adhere to the tooth surface. Here we present the X-ray structure of FimP, the protein that is polymerized into the type-1 pilus stalk, assisted by a pili-specific sortase. FimP consists of three tandem IgG-like domains. The middle and C-terminal domains contain one autocatalyzed intramolecular isopeptide bond each, a feature used by Gram-positive bacteria for stabilization of surface proteins. While the N-terminal domain harbours all the residues necessary for forming an isopeptide bond, no such bond is observed in the crystal structure of this unpolymerized form of FimP. The monomer is further stabilized by one disulfide bond each in the N- and C-terminal domains as well as by a metal-coordinated loop protruding from the C-terminal domain. A lysine, predicted to be crucial for FimP polymerization by covalent attachment to a threonine from another subunit, is located at the rim of a groove lined with conserved residues. The groove may function as a docking site for the sortase-FimP complex. We also present sequence analyses performed on the genes encoding FimP as well as the related FimA, obtained from clinical isolates.

Place, publisher, year, edition, pages
2012. Vol. 7, no 10, e48364- p.
Keyword [en]
crystal structure, pili
National Category
Structural Biology Biochemistry and Molecular Biology
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:umu:diva-61474DOI: 10.1371/journal.pone.0048364OAI: oai:DiVA.org:umu-61474DiVA: diva2:568026
Funder
Swedish Research Council
Available from: 2012-11-15 Created: 2012-11-15 Last updated: 2017-12-07Bibliographically approved

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Publisher's full texthttp://dx.plos.org/10.1371/journal.pone.0048364.

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