ArticlePloS one2012
The pilin protein FimP from Actinomyces oris: crystal structure and sequence analyses.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Type IV pili ofEcoSal Plus · 2024Review
- The basal and major pilins in the Corynebacterium diphtheriae SpaA pilus adopt similar structures that competitively react with the pilin polymerase.Biopolymers · 2024Article
- Domain structure and cross-linking in a giant adhesin from the Mobiluncus mulieris bacterium.Acta crystallographica. Section D, Structural biology · 2023Article
- Electron cryo-microscopy reveals the structure of the archaeal thread filament.Nature communications · 2022Article
- Enigmatic Pilus-Like Endospore Appendages ofInternational journal of molecular sciences · 2021Review
- Secretome profiling of Propionibacterium freudenreichii reveals highly variable responses even among the closely related strains.Microbial biotechnology · 2018Article
- Bent conformation of a backbone pilin N-terminal domain supports a three-stage pilus assembly mechanism.Communications biology · 2018Article
- Engineering a Lys-Asn isopeptide bond into an immunoglobulin-like protein domain enhances its stability.Scientific reports · 2017Article
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.Journal of bacteriology · 2015Review
- A Disulfide Bond-forming Machine Is Linked to the Sortase-mediated Pilus Assembly Pathway in the Gram-positive Bacterium Actinomyces oris.The Journal of biological chemistry · 2015Article
- Article
- Structural conservation, variability, and immunogenicity of the T6 backbone pilin of serotype M6 Streptococcus pyogenes.Infection and immunity · 2014Article
- Structural basis of pilus anchoring by the ancillary pilin RrgC of Streptococcus pneumoniae.The Journal of biological chemistry · 2014Article
- A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Structure of the C-terminal domain of AspA (antigen I/II-family) protein from Streptococcus pyogenes.FEBS open bio · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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