Superposition of FimP and FimA.

<p>The FimP crystal structure superimposed onto the corresponding structure of FimA (M- and C domains). The FimP structure is depicted in light blue and FimA in green. The proline-rich segment in FimA is coloured in orange with the prolines as stick models. The equivalent loop in FimP is colored in purple. The metal ion coordinated by a FimP loop is depicted in grey. The N-terminal domain of FimP is colored in light grey. The figure is shown in stereo.</p

Data collection, refinement and model quality statistics for FimP.

a<p>Values in parentheses indicate statistics for the highest resolution shell.</p>b<p><i>R</i>_sym = Σ<i>_hkl</i> Σ<i>_i</i> |<i>I</i>_i<i>(hkl)</i>−<<i>I</i>(<i>hkl</i>)>|/Σ<i>_hkl</i> Σ<i>_i I</i>_i (<i>hkl</i>), where <i>I_i</i>(<i>hkl</i>) is the intensity of the <i>i</i>th observation of reflection <i>hkl and </i> is the average over of all observations of reflection <i>hkl.</i></p>c<p><i>R</i>_work = Σ | |<i>F</i>_obs|−| <i>F</i>_calc| |/Σ | <i>F</i>_obs|, where <i>F</i>_obs and <i>F</i>_calc are the observed and calculated structure factor amplitudes, respectively. <i>R</i>_free is <i>R</i>_work calculated using 5% of the data, randomly omitted from refinement.</p

Domains and topology diagram.

<p>Each domain (N-, M- and C-) with labeled secondary structure. <b>A:</b> N-domain in coral, <b>B:</b> M-domain in light blue, <b>C:</b> C-domain in blue. The Ca²⁺ ion is depicted as a magenta sphere. <b>D:</b> Topology diagram of FimP with domains colored as in <b>A</b>–<b>C</b>. The isopeptides are depicted as red, and disulfides as green, bars. The Ca²⁺ ion coordinated by the loop is shown as a grey sphere.</p

Mass determination of wild type and mutant FimP_31–491 proteins.

a<p>MS, ESI-TOF mass spectrometry.</p

The pilin motif forms a groove.

<p>Stereo representation of the pilin motif residues lining a cleft that runs through the N-domain. Lys-182, involved in polymerization of FimP subunits, is localized at the rim of the cleft. The domain is presented as a semi-transparent electrostatic surface, colored in red and blue according to negative and positive electrostatic potential, respectively. The residues in the pilin motif are shown as stick models. The groove is highlighted with a dashed line.</p

Domain architecture of FimP.

<p>The FimP protein is comprised of a signal peptide (SP), an N-terminal domain, a middle domain and a C-terminal domain followed by an LPXTG motif and a transmembrane domain (TD). Residues involved in isopeptide and disulfide bonds are illustrated with bars and stars, in red and green, respectively. A lysine and a threonine involved in pili polymerization are illustrated with a green and black diamond respectively.</p

Sequence analyses of FimP and FimA among <i>A. oris</i> isolates.

<p><b>A:</b> Sequence alignment of FimP (n = 48) with fully conserved isopeptide bond triads (red), disulfide bonds (green), a conserved metal binding loop (grey) and pilin-, E-box- and LPLTG motifs in yellow. <b>B:</b> Sequence alignment of FimA (n = 14) with fully conserved isopeptide bond triads (red), disulfide bonds (green), a conserved proline-rich loop (blue) and pilin-, E-box- and LPLTG motifs in yellow. In addition, in A and B, polymorphic amino acid residues are shown (single letter codes). The top lines represent the consensus sequence and amino acid positions based on FimP and FimA respectively of reference strain T14V. <b>C:</b> Neighboring joining tree with sixteen allelic or sequence <i>fimP</i> types among <i>A. oris</i> isolates (n = 48) due to the single amino acid variations.</p

Stabilizing isopeptide bonds (formed and unformed) and a metal binding loop.

<p><b>A:</b> The putative isopeptide residues in the N-domain, Lys-52, Asn-183 and Glu-145, do not form an isopeptide bond in the crystal structure. <b>B</b>: The M-domain isopeptide bond formed between Lys-190 and Asn-319 with the catalytic Asp-230. Asp-230 forms a bidentate hydrogen bond with the isopeptide bond. <b>C:</b> The C-domain isopeptide bond formed between Lys-363 and Asp-487 with the catalytic Glu-452. Glu-452 forms one hydrogen bond with the isopeptide bond carbonyl oxygen. <b>D:</b> A Ca²⁺ ion is coordinated by five residues of a loop that protrudes from the C-domain. Residues involved in isopeptide bond formation are represented as stick models, colored by atom type in a simulated annealing, omit Fo-Fc maps contoured at 4σ. Hydrogen bonds are shown as broken lines. Surrounding hydrophobic residues are shown as stick models.</p

Innate immunity glycoprotein gp-340 variants may modulate human susceptibility to dental caries-5

<p><b>Copyright information:</b></p><p>Taken from "Innate immunity glycoprotein gp-340 variants may modulate human susceptibility to dental caries"</p><p>http://www.biomedcentral.com/1471-2334/7/57</p><p>BMC Infectious Diseases 2007;7():57-57.</p><p>Published online 11 Jun 2007</p><p>PMCID:PMC1894970.</p><p></p> caries-associated variables from modelling with caries experience in the children as dependent variable, and (B) gp-340 I to III phenotypes from modelling with saliva adhesion of in the children as dependent variable

Innate immunity glycoprotein gp-340 variants may modulate human susceptibility to dental caries-4

<p><b>Copyright information:</b></p><p>Taken from "Innate immunity glycoprotein gp-340 variants may modulate human susceptibility to dental caries"</p><p>http://www.biomedcentral.com/1471-2334/7/57</p><p>BMC Infectious Diseases 2007;7():57-57.</p><p>Published online 11 Jun 2007</p><p>PMCID:PMC1894970.</p><p></p>stern blotting of parotid saliva samples with mAb143. Unreduced parotid saliva samples were separated by SDS-PAGE on 5% gels. Molecular masses (kDa, left) and gp-340 I to III phenotype (top) of the three saliva donors are marked