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. Author manuscript; available in PMC: 2021 May 21.
Published in final edited form as: Cell Chem Biol. 2020 Mar 19;27(5):560–570.e10. doi: 10.1016/j.chembiol.2020.02.007

Figure 4. Characterization of the Binding of JSF-3285 to KasA through X-Ray Crystallography and MST Assay.

Figure 4.

(A) Left: KasA dimer with one protomer (KasA) rendered as a blue surface and the other protomer (KasA′) rendered as an orange cartoon. The JSF-3285 molecules are shown as green and light blue stick models. Right: expanded view of area enclosed in the yellow rectangle in the left panel with one KasA protomer hidden for clarity. Residues that are within 4.0 Å of JSF-3285 are depicted as blue sticks. Black, dashed lines indicate hydrogen bonds between KasA and JSF-3285 measured in angstroms.

(B) Schematic representation of KasA-JSF-3285 interactions. Hydrogen bonds are depicted as dashed lines measured in angstroms. The blue semicircles with radiating lines represent hydrophobic contacts mediated by KasA residues. The schematic was produced with LIGPLOT.

(C) MST quantification for JSF-3285 binding to KasA. JSF-3285 was titrated between 0.0209 and 300,000 nM with 50 nM labeled KasA. JSF-3285 binds to KasA with a Kd = 70.7 ± 23.5 nM. Data presented as the mean ± standard deviation of three independent assays.