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Overall and active site structure of E. coli AlaA in complex with acetate.

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posted on 11.07.2014, 02:53 by Esther Peña-Soler, Francisco J. Fernandez, Miguel López-Estepa, Fernando Garces, Andrew J. Richardson, Juan F. Quintana, Kenneth E. Rudd, Miquel Coll, M. Cristina Vega

(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.

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