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![[Figure 1]](gri5002fig1mag.jpg)
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Figure 1
The structure of the ΔP1 pilin with important residue interactions highlighted (PDB entry 8v7p). (a) The ΔP1 pilin monomer; the N-terminal α-helix (α1-C) is in blue, the β-sheet is in green and the coil regions are in purple. The disulfide between Cys127 and Cys145 is shown in yellow and the cacodylic acid molecule is shown as sticks with atomistic coloring. (b) A portion of the hydrophobic interface seen between the α1-C helix, the β-meander and the α–β loop. Side chains of the hydrophobic residues (orange) are pointed towards the interior of the molecule to create a hydrophobic pocket. At 1.3 Å resolution numerous solvent contacts were seen in the ΔP1 structure, including the hydrogen-bonding network (dotted yellow lines) containing a water molecule (in red) seen in (c) which aids in maintaining the conformation of the α–β loop. (d) A view of the bend in the α1-C helix and the hydrogen bonding between the conserved Trp125 and Glu48, as well as the backbone of Gly123 and water 55, which stabilizes the kinked α-helix. (e) The receptor-binding D-loop; residues making hydrogen bonds supporting the disulfide bond. Cys127 is depicted with its reduced conformer and Pro146 is shown with both endo and exo conformers. (f) ΔP1 is colored via B factor, with low to high B factors set from blue to red (5–22 Å2). The highest B factors are in the α–β loop and hypervariable loop regions on the side opposite to the RBD, with some dynamics seen in the RBD. All images were generated using PyMOL version 2.5.0 (Schrödinger). |
![[Figure 1]](gri5002fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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