Fig. 3: 2OG binding site and structural rearrangement in MtGS.

a Close-up of the 2OG binding site in MtGS (cyan cartoon, the adjacent monomer in light blue) shown as a stereo view. 2OG and the residues in its vicinity are shown as balls and sticks with contacts in black dashes. b, c Same view as in (a) showing MsGS apo ((b) purple cartoon, with the adjacent subunit in light purple) and BsGS apo ((c) red cartoon, with the adjacent subunit in light red, PDB 4LNN). 2OG from MtGS (gray) was superposed to visualize the clash with E89’ for MsGS and E36’/Y20’ for BsGS. d Sequence alignment of different GSI-α in which 2OG-binding residues observed in MtGS are highlighted with a cyan box (see Fig. S11 for the entire alignment). e Structural rearrangements between the apo (gray cartoon) and 2OG/Mg²⁺/ATP bound state (cyan cartoon). The adjacent monomer is colored lighter. Phe18’ is shown as sticks. Arrows highlight the movements caused by 2OG binding. f MtGS apo (gray cartoon) superposed to MtGS-2OG/Mg²⁺/ATP (cyan cartoon). The superposition was done on one monomer (indicated by an arrow), and a dashed line was drawn on the Cα position of Val4, Gly198, and Asn267 to illustrate the overall movements. For all, oxygen, nitrogen, and phosphorus are colored in red, blue, and orange, respectively. Carbons are colored depending on the chain and in yellow for ligands.