Skip to main content
. 2010 Sep 17;285(48):37753–37761. doi: 10.1074/jbc.M110.122804

FIGURE 2.

FIGURE 2.

Structure of the chitobiose-OmpA (WT) complex after 70 ns of MD in explicit solvent, counter ions, and membrane. The binding sites are indicated by the electrostatic surface plots. These MD studies started with the two structures from docking: pose L (for loops) with chitobiose bound to loops 1, 2, and 3) and pose B (for barrel) with chitobiose bound to loop 4. Upper right panel, L binding site, showing all residues within 4 Å. Here three of the four HBs are shown, two of which are removed upon mutation (1a and 2c mutants). The average interaction distance is indicated in angstroms. The average deviation is 0.2 Å. Red arrows, hydrogen bond between chitobiose and protein; chitobiose is proton donor. Green arrows, hydrogen bond; chitobiose is proton acceptor. Lower right panel, B binding site, showing all residues within 4 Å. There is a strong HB to Thr-153, which is removed in the 4b mutant. Trp-103 has three strong electrostatic interactions with the C5 alcohol and O6 motifs of chitobiose. Thr-145 has two weak hydrogen bond interactions.