Fig. 7: Structural insights into the recognition of malonyl-ACP by the BioZ enzyme.

a Structural display of the ACP moiety of acyl-ACP substrate bound to the paradigm enzyme of FAS I, the E. coli FabB. b An enlarged view of the ACP-interacting interface of FabB that is constituted by six positively-charged residues. The image is generated through a counter-clockwise 90° rotation of the rectangle-dashed lined region (a). c Binding model of glutaryl-ACP to the positively-charged surface of AtBioZ. ACP is given in ribbon structure colored gray, which comprises four α-helices (helix-1 to helix-4). The interface of FabB (a) [and/or BioZ (c)] interacting with ACP group is illustrated in the surface electrostatic structure. The blue denotes positive charge, whereas the red refers to negative charge. d Visualization of the putative ACP-binding domain of BioZ. Presumably, it contains four basic residues, namely R39, R153, R221, and R260. This image is given through the counter-clockwise 90° rotation of the square-dashed lined region (c). e Growth curve-based assay to probe the role of the putative four basic residues-comprising, ACP-binding interface in the BioZ function. The strains used here were listed in Supplementary Table 1, and the growth curve was plotted as described in Fig. 5e. A representative result was given.