Fig. 2: MO/RBD interaction facilitates the activity inhibition of MICAL1.
From: Autoinhibition and relief mechanisms for MICAL monooxygenases in F-actin disassembly
a–c The MO/RBD interaction observed in the autoinhibited MICAL1 structure (a), highlighting the critical interactions at the MOL/RBD (b) and MOS/RBD (c) interfaces. d–f Structural comparisons showing conformational differences in the MO domain of autoinhibited MICAL1 (d) compared to the MO fragments in oxidated (MOox, PDB: 2BRY) (e) or reduced (MOred, PDB: 2C4C) (f) conditions. The binding of the RBD to the MO limits the conformational changes of FAD and the surrounding loops. g Schematic diagram illustrating the inhibitory mechanism of the MO domain by the RBD. h NADPH-consumption measurements of MICAL1 and the MO/RBD interface mutants. Protein concentration of 1 μM was used. Three independent repeats were performed for each condition. i Confocal imaging of HeLa cells overexpressing GFP-tagged MICAL1 and the MO/RBD interface mutants. Actin filaments were stained by fluorescence-labeled phalloidin. Cell edges were indicated by dashed lines for reference.
