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Figure 5.
FIGURE 5. Interactions between FabI and ACP. A,
interactions between ACP (cyan) and FabI (green) at the helix
 2
(ACP)-helix 8 (FabI) interface. B,
interactions between crotonyl-pantetheine and FabI. The
pantetheine (cyan) is hydrogen bonded to residues in FabI helix
8
(green). FabI residues in the conserved active site triad
(Tyr^146, Tyr^156, and Lys^163) are colored yellow. The crotonyl
group of the substrate (cyan) is bound in the s-trans
conformation and the crotonyl carbonyl group is oriented toward
Tyr^146 (yellow). The C-3 carbon of the crotonyl group is 3
Å from the NADH pro4(S) proton (white). In addition, the
NADH ribose (cyan) is hydrogen bonded to Tyr^156 and Lys^163.
The figure was made with pymol (64).
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