Fig. 3: Structural and functional studies on Pgp3 in complex with BMK-S201 and its derivatives.
From: Structure-based inhibitor design for reshaping bacterial morphology
a Chemical structures of BMK-S201 and its derivatives, BMK-S202 and BMK-S203. Green, red, purple, and cyan circles indicate the Y-Y binding motif, hydrophobic pocket binding motif, Zn binding motif, and linker motif, respectively. b–d The ITC fitting results of Pgp3 with (b) BMK-S201, (c) BMK-S202, and (d) BMK-S203. The thermodynamic data were collected from titration of each inhibitor into Pgp3, and the parameters were calculated by fitting to a single-binding model. e–g Detailed interaction of Pgp3 H247A active sites bound with (e) BMK-S201 (orange), (f) BMK-S202 (olive), and (g) BMK-S203 (bright orange). Key interaction residues in Pgp3 are colored with light blue, whereas Zn2+ ion and water molecules are represented by blue and slate gray spheres, respectively. The coordination of Zn2+ and hydrogen bonds are represented by black dashed lines. Light blue circle with dashed line represents the Y–Y binding region.
