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. 2008 Jul 22;105(30):10348–10353. doi: 10.1073/pnas.0803039105

Fig. 3.

Fig. 3.

Binding site for NAM. (A) (2mFo-DFc) sigmaA-weighted (27) electron density for NAM bound to MotB-C. The map was calculated at 2.3-Å resolution and contoured at 0.7-σ level. (B) Locations of the MotB-C residues structurally equivalent to the functionally important residues in E. coli MotB (named in parentheses): Ala-128 (Gly-164), Thr-163 (Thr-196), Asp-164 (Asp-197), Arg-172 (Glu-205), Ala-180 (Ser-214), Arg-183 (Arg-217), Met-188 (Arg-222), Gly-207 (Gly-240), Thr-209 (Ala-242), and Arg-226 (Arg-258). The positions of the Cα atoms of the residues with buried side chains are shown in blue, and surface-exposed chains are in red. (C) Stereoview of the molecular surface of MotB-C in the vicinity of the bound NAM molecule showing the putative glycan chain binding groove. The positions of residues Arg-172 and Thr-209 are highlighted. (D) View of the MotB-C dimer, as found in the crystal structure. The position of the bound NAM is shown for both monomers.