Fig. 2: The structure of FimTLp.
From: The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation
a The solution structure of FimTLp 28–152 (state 18) in ribbon representation (left) and the corresponding topology diagram (right). Secondary structure elements are indicated: truncated N-terminal α-helix (α1C) (blue), β-sheet I formed by β1, β2, β3, and β5 (yellow), and β-sheet II formed by β4, β6, and β7 (magenta). A vertical arrow indicates the pilus axis from the cell surface towards the pilus tip. b Structure alignment of FimTLp (blue) and FimUPa (grey; PDB ID: 4IPV) (left) and the topology diagram of FimUPa (right). The disulphide bond of FimUPa is indicated in stick representation with sulphur atoms in yellow. c Superimposed 20 lowest energy structures calculated by NMR spectroscopy. An arrow indicates the conformational flexibility of the C-terminal tail (140–152). The pairwise backbone root-mean-square deviation (RMSD) for the structured region (residues 32–62, 70–139) is 1.13 Å. N- and C-termini are indicated in each panel. d Cα chemical shift values (top) and T2(1H) transverse relaxation data (bottom), encompassing the last 27 residues of FimTLp. Secondary structural elements are indicated and error bars represent the fitting errors of the respective exponential decay curves. Source data are provided as a Source Data file.
