Fig. 3: CXE15 dimerisation is stabilised by oxidation-induced disulphide formation at C14.
From: Molecular Basis for Catalysis and Regulation of the Strigolactone Catabolic Enzyme CXE15
A Fit of the SAXS experimental data (blue dots) for monomeric (left) and dimeric (right) peak fractions with the scattering pattern calculated for the monomeric (red) and dimeric (green) structural models shown below. Particle parameters from the SAXS data are shown in Supplementary Fig. 7E. B Thermal melting curve for CXE15 and the CXE15 C14S mutant treated with H2O2 in the presence and absence of DTT. The experiments were repeated three times independently. C YLG hydrolysis activity of CXE15 and its mutants. Data are presented as mean values ± SEM from three independent replicates. D Thermal melting curve for CXE15 and the CXE15 C14S mutant in the presence and absence of GR24. The experiments were repeated three times independently.
