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. Author manuscript; available in PMC: 2014 Apr 2.
Published in final edited form as: Biochemistry. 2013 Mar 19;52(13):2280–2290. doi: 10.1021/bi400097z

Fig. 6.

Fig. 6

Active sites of ATP-bound A. aeolicus LpxK in the “open form”. (A) Simulated annealing omit electron density for ATP and MPD (mesh) in the ATP-bound structure was calculated using coefficients Fo – Fc, contoured at 4 σ. The “bent” ATP molecule is bound to the “open”, normally apo conformation of the enzyme. Dashed lines indicate hydrogen bonds. (B) Stereo view of the overlay of AMP-PCP (cyan) and ATP (magenta) bound LpxK structures reveals a shift in nucleotide binding upon domain closure. Side chains and hydrogen bonds are colored accordingly. Side chain rotation of F296 between the two structures is indicated with an arrow.