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1.
Figure 1

Figure 1. From: Slow-Onset Inhibition of the FabI Enoyl Reductase from Francisella Tularensis: Residence Time and In Vivo Activity.

Structure of Triclosan and the Diphenyl Ether ftuFabI Inhibitors.

Hao Lu, et al. ACS Chem Biol. ;4(3):221-231.
2.
Figure 6

Figure 6. Linear Correlation between Percent Survival and Residence Time. From: Slow-Onset Inhibition of the FabI Enoyl Reductase from Francisella Tularensis: Residence Time and In Vivo Activity.

A linear fit to the data from Table 2 for compound residence time and percent survival in an animal model of infection gave a straight line with r=0.99.

Hao Lu, et al. ACS Chem Biol. ;4(3):221-231.
4.
Figure 4

Figure 4. Survival Plots for Compounds 1, 4, 8, 9 and 11. From: Slow-Onset Inhibition of the FabI Enoyl Reductase from Francisella Tularensis: Residence Time and In Vivo Activity.

Survival plots for mice infected with F. tularensis Schu4 and treated with compounds 1, 4, 8, 9 and 11.

Hao Lu, et al. ACS Chem Biol. ;4(3):221-231.
5.
Figure 5

Figure 5. Progress Curve Analysis of the Inhibition of ftuFabI by Compound 10. From: Slow-Onset Inhibition of the FabI Enoyl Reductase from Francisella Tularensis: Residence Time and In Vivo Activity.

(A) Time-dependent inactivation of ftuFabI by compound 11. The solid curves represent the best fit of the data to equation 7 for slow onset inhibition. (B) kobs values from A plotted as a hyperbolic function of [I].

Hao Lu, et al. ACS Chem Biol. ;4(3):221-231.
6.
Scheme 1

Scheme 1. Kinetic Schemes for the Interaction of ftuFabI with Inhibitors. From: Slow-Onset Inhibition of the FabI Enoyl Reductase from Francisella Tularensis: Residence Time and In Vivo Activity.

(A) Inhibitor binds exclusively to the E-NAD+ form of the enzyme with an equilibrium dissociation constant of Kii. (B) Inhibitor binds to both E-NAD+ and E-NADH forms of the enzyme with equilibrium dissociation constants of K1 and K2, respectively. (C) Slow onset inhibition of ftuFabI in which formation of the final E-I* inhibitor complex occurs in two steps, the second of which is the slow step.

Hao Lu, et al. ACS Chem Biol. ;4(3):221-231.
7.

Figure 2. X-ray Structures of ecFabI and ftuFabI. From: Slow-Onset Inhibition of the FabI Enoyl Reductase from Francisella Tularensis: Residence Time and In Vivo Activity.

(A) Ribbon presentation of E. coli FabI with a close up view of the active site. The carbon atoms of the triclosan molecule are shown in black and in the NAD+ molecule in blue. Oxygen atoms are depicted in red, chloride atoms in green, nitrogen in blue and phosphorous in orange. (B) Loop ordering upon triclosan binding. The left panel shows the E. coli FabI (pdb code 1dfi) with bound NAD+ (blue) with the loop ends marked in red. The second panel shows the ternary triclosan-NAD+ E. coli FabI structure (pdb code 1qg6) with the loop ordered into a helix (amino acids 194 – 201 shown in red). (C) Superposition of E. coli FabI with bound NAD+, both shown in cyan and F. tularensis FabI shown in brown with bound NAD+ (yellow). In both structures the active site loop is disordered, the loop ends are marked in red. Superpositions were calculated with Superpose using secondary structure matching (43) implemented in the ccp4 program suite (44). All model illustrations were prepared with PyMOL (45).

Hao Lu, et al. ACS Chem Biol. ;4(3):221-231.

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