Fig. 2

a Structural superimposition of ZG180/SaClpP and ZG180/HsClpP complexes to reveal the strategy for designing selective activators for SaClpP over HsClpP. SaClpP and HsClpP are shown in gray and wheat cartoon tubes, respectively. ZG180 is colored in cyan in the ZG180/SaClpP structure, while it is colored in yellow in the ZG180/HsClpP structure. I91 in SaClpP and W146 in HsClpP are shown as a stick. b Structures of SaClpP activators (R)- and (S)-ZG197 developed by the structure-based design outlined in (a). The chiral methyl group is indicated in red. c Quantitation of α-casein hydrolysis by SaClpP and HsClpP in the presence of (R)- and (S)-ZG197, respectively (n = 3 biologically independent experiments). Data are presented as mean ± SD (error bars). d Effect of activators on degradation of the cellular SaFtsZ protein with the supplement of bovine serum albumin (BSA), the recombinant SaClpP, and HsClpP, respectively, in cell lysates of the clpP deletion (ΔclpP) mutant. The abundance of cellular SaFtsZ is quantitated with a Western blot assay. Quantitation on the band intensity of SaFtsZ is normalized against the loading control of SaGAPDH, and the ratio in the DMSO group is considered as 1.0. Source data are provided as a Source Data file.