Fig. 1: Structural basis of controlled SL hydrolysis by CXE15.
From: Molecular Basis for Catalysis and Regulation of the Strigolactone Catabolic Enzyme CXE15
A The monomeric crystal structure of CXE15 (black) superimposed on a single chain of its dimeric form (core: green; N-terminal extension: grey). Catalytic residues are highlighted in magenta and encircled. Cys14 is shown in orange. B The dimeric form of CXE15. The first molecule is coloured as in (A), and the second molecule is in dark green with its N-terminal extension in black. The catalytic residues on one chain are shown in magenta and encircled. C Superimposition of the N-terminal helices of the CXE15 dimer (grey) over the helices of the CXE15 C14S mutant (cyan). Both Cys14 involved in disulphide bond formation are depicted as orange sticks with a prime (‘) denoting the second chain. D Superimposition of the CXE15 monomer (green, from the dimeric form) with rice D14 (PDB: 6elx, light brown). E A zoomed-in view of the superimposed catalytic sites shown in (D). F GR24 (cyan sticks) docked to the CXE15 dimeric structure [coloured as in (B)]. Residues interacting with GR24 are shown as sticks.
