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. 2022 May 25;13(1):246–255. doi: 10.1016/j.apsb.2022.05.022

Figure 1.

Figure 1

The crystal structure of DgpA in an auto-inhibited conformation. (A) Free enzyme crystal structure of DgpA in homo-hexameric (PDB ID: 7XRE) and each DgpA subunit is differently colored. NAD+ is displayed in stick and ball model in orange. (B–C) Representative homo-tetrameric structure (B) (PDB ID: 6a3j) or homo-dimeric structure (C) (PDB ID: 5a03) of NAD(H)-dependent oxidoreductase in Gfo/Idh/MocA family. (D) The loop that locks DgpA in an auto-inhibited conformation from the neighboring subunit is highlighted using thick purple dashed box. (E) Close-up view of the inhibiting loop with key residues in yellow bound to DgpA substrate recognition pocket with key residues in cyan. (F) The effect of the loop deletion on the glucose oxidation increase by DgpA in a glucose oxidation experiment. Two loop deletion mutants are in red bar diagram and the wild type or loss function D182A mutant are in black. The DCPIP concentration was calculated from the standard calibration curve of reference DCPIP.