Fig. 3

Key features of PGAM5 activation in the crystal structure of ∆90 PGAM5 H015A/MM. a The structures of ∆90 PGAM5 H105A with the multimerization motif (MM) added in trans (∆90 PGAM5 H105A/MM) (left panel) compared to the structures of ∆90 PGAM5 (PDB: 3MXO) (middle panel) and ∆54 PGAM5 with the MM present in cis (PDB: 5MUF) (right panel). Monomers 1 and 2 are colored cyan and light blue, respectively, in all structures with their corresponding MM regions colored in teal (monomer 1 MM) and dark blue (monomer 2 MM) where present. The β1–α1 loop is indicated in orange, the β3–α3 loop is indicated in green, the α3–β4 loop is indicated in red. The F244 residues in the central axis forming the dimer interface are indicated in yellow. b Detailed view of the catalytic core in ∆90 PGAM5 H105A/MM (left), ∆90 PGAM5 (middle), and ∆54 PGAM5 (right) highlighting interactions between active-site residues and the phosphate ion (PO₄). c, d Comparison of the MM architecture (left panel) and the differences in interactions with the phosphatase domain (right panel) for c ∆90 PGAM5 H105A/MM and d ∆54 PGAM5