N-PilO2_Bp protein.

<p><b>A.</b> Overall fold of N-PilO2_Bp composed of two α/β topology subdomains, each displaying a mixed β-sheet, separated by a (central) cleft. The bound phosphate ion is shown as spheres. <b>B.</b> Topology diagram of N-PilO2_Bp. This diagram was generated using PDBSum server (<a href="http://www.ebi.ac.uk/pdbsum/" target="_blank">www.ebi.ac.uk/pdbsum/</a>) <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0094981#pone.0094981-Laskowski2" target="_blank">[52]</a>. <b>C</b>. Crystal packing of the phosphate-containing N-PilO2_Bp structure, showing the three crystal packing dimers formed by alternative interactions between four symmetry-related monomers (green, blue, magenta and black). The three interfaces are highlighted by black, blue and red shading. The first ‘dimer’, is formed by the interaction between the green (or blue) and the magenta (or black) monomers and the light green (or light blue) phosphate. The second crystallographic dimer occurs between the magenta and black monomers. The third dimer is formed by the green and blue monomers. <b>D</b>. Stereo view of the electron density map for the residues building the phosphate ion binding pocket. The phosphate ion is shown as sphere; the electron density is contoured at 1.5 sigma level. <b>E.</b> Front and back view of N-PilO2_Bp electrostatic surface potential. The electrostatic potential was calculated using the CCP4MG viewer. Negative (red) and positive (blue) charges, and uncharged (white) surfaces are shown. <b>F.</b> Superposition of the 3D structures of N-PilO2_Bp (cyan; PDB codes 4BYZ and 4BZ0) and N-BfpC (chocolate; PDB code 3VHJ).</p

Crystallographic data-collection statistics.

a<p>Data completeness treats Bijvoët mates independently.</p>b<p>Statistics for the highest resolution shells are given in parentheses.</p>c<p><i>R</i>_merge = ∑<i>_hkl</i>∑<i>_i</i>|<i>I(hkl)_I</i> − < <i>I(hkl)</i> >|/∑<i>_hkl</i>∑<i>_i</i>< <i>I(hkl)_i</i> >.</p>d<p>Substructure determination parameters are from ShelxD.</p>e<p>CC  =  [∑<i>wE_oE</i>_c∑<i>w</i> - ∑<i>wE_o</i>∑<i>wE_c</i>]/{[∑<i>w</i>E_o²∑<i>w -</i> (∑<i>w</i>E_o)²] [∑<i>w</i>E_c²∑<i>w</i> -(∑<i>w</i>E_c)²]}^1/2,</p><p>where <i>w</i> is weight. CC_all/CC_weak is the correlation coefficient for all and weak reflections of the best solution.</p>f<p>FOM, figure of merit  =  | <i>F</i>(<i>hkl</i>)best|/|<i>F</i>(<i>hkl</i>)|; <b>F</b>(<i>hkl</i>)best  =  ∑<i>P</i>(α)<b>F</b>_hkl(α)/∑<i>P</i>(α).</p

Comparison of Tfpb machinery R64 thin pilus variant encoding operons for different microorganisms.

<p>The alignment was performed using tblastx from the Blast suite, and visualized in Artemis Comparison Tool. Conserved protein regions are paired by color-shaded regions; the blue and red colors represent the reverse and forward matches, respectively, and color intensity is proportional to the sequence homology. Genes are represented by arrows; the same arrow color indicates putative orthologs. The grey arrows represent genes lacking homologs among represented <i>pil</i> clusters. The <i>pil</i> cluster sequences were retrieved from GenBank: <i>Tfp7</i> locus from <i>B. pseudomallei</i> (<i>Bp</i>) chromosome 2 complete sequence, BX571966.1; PAPI-1 <i>pil</i> gene cluster from <i>P. aeruginosa</i> (<i>Pa</i>) PA14, AY273869.1; R64 transfer region, AB027308.1; and <i>pil</i> operon from <i>Salmonella enterica</i> (<i>Se</i>) subsp. <i>enterica</i> serovar Paratyphi C strain CN13/87, AY249242.1.</p