Overall and active site structure of E. coli AlaA in complex with acetate.
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(A) Ribbon representation of the overall structure of AlaA. One of the chains is shown in green while the other is shown in domain colors: the central, large domain in cyan, the small domain in violet, and the N-terminal arm of both chains is shown in deep blue. The PLP cofactor is shown in spheres and CPK colors. (B) Detail of the interaction between the N-terminal arm (H1-plug-H2) motif of one AlaA subunit (green) with helix H4 from the other subunit (cyan), shown with the experimental σA-weighted electron density map (2mFo–DFc) contoured at 1.0 σ level. Relevant helices and residues that participate in the interaction are labeled. (C) Inset of the active site. Active site residues are shown in sticks and color-coded as in (B); the carbon atoms of Lys240-PLP are in grey and in yellow in the acetate anion. Polar interactions within 3.5 Å of the PLP cofactor and acetate are represented by dotted lines. The experimental σA-weighted electron density map (2mFo–DFc) contoured at 1.0 σ.