Figure 1
Structural differences between DraD/AfaD and DraE/AfaE fimbrial subunits. (A) Topology diagram of DraD-DraE tip complex. The core forming strands are striped, the S-S denotes disulfide bond. (B) Comparison of DraD-sc and DraE-sc acceptor cleft area. In both proteins A and F strands forming the groove as well as the donor Gd strand are shown as ribbons. Backbone hydrogen bonds participating in the β-barrel formation are drawn as blue springs. (C) Tyrosine corner joining E and F strands. Residues of the canonical tyrosine corner motif are drawn as thick sticks while side chains of residues comprising the hydrophobic core of the protein as thinner sticks. Arg16 moiety completely buried in the core of DraE protein is drawn with thicker line. The figures were generated with VMD program (Theoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign) [42].