Fig. 2: CXE15 dimerisation is stabilised by the N-term residues.
From: Molecular Basis for Catalysis and Regulation of the Strigolactone Catabolic Enzyme CXE15
A Root-mean-square fluctuation (RMSF) analysis of residues 9–40 from CXE15 using molecular dynamics simulations for the monomeric and dimeric forms, along with their respective mutants. B Root-mean-square deviation (RMSD) profiles of CXE15 residues calculated from molecular dynamics simulations for the monomeric and dimeric forms, including their respective mutants. C RMSD and RMSF values for the CXE15 monomer, dimer and its mutants. Data are expressed as mean values ± SEM. The data shown in panels A, B were repeated three times independently. D MST curve for dimerisation of CXE15 or the CXE15 C14S mutant in the presence and absence of GR24. The Kd values are given in square brackets and the data are presented as mean values ± SEM from three independent replicates. E Yeast two-hybrid screening to identify binding partners of CXE15 and its mutants (n = 1). F YLG hydrolysis activity of CXE15 and its dimer mutants. Data are presented as mean values ± SEM from three independent replicates. G Non-reducing SDS-PAGE gel for CXE15 and the CXE15 C14S mutant treated with H₂O₂ in the presence and absence of DTT. Samples represent SEC fractions as shown in Supplementary Fig. 7B. The experiments were repeated three times independently.
