Fig. 6: Structural and functional analysis of BioZ binding to malonyl-ACP. | Nature Communications

Fig. 6: Structural and functional analysis of BioZ binding to malonyl-ACP.

From: Biochemical and structural characterization of the BioZ enzyme engaged in bacterial biotin synthesis pathway

Fig. 6

Surface structure (a) and ribbon illustration (c) of the FabB dimer crosslinked with ACP. It was generated with PyMol using crystal structure of FabB-ACP (PDB: 5KOF). Surface structure (b) and ribbon illustration (d) of the dimeric BioZ complexed with malonyl-ACP. e Use of isothermal titration calorimetry (ITC) to probe the interaction between malonyl-ACP and BioZ. A representative result of ITC is shown, and the resultant stoichiometry values (N and Kd) from three independent experiments are given in an average ± SD. The putative binding mode of BioZ to its substrate malonyl-ACP (and/or glutaryl-ACP) was generated through structural superposition. The stoichiometry (malonyl-ACP: BioZ) is 1:1, in that the molar ratio was measured to be ~0.996. The parameter of binding affinity (Kd) is 24.133 ± 0.602 μM.

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