mechanism shows an enzyme-catalyzed formation of a high-energy imidazolate intermediate. Changes in manganese coordination chemistry dominate all aspects of catalysis. In the first part of the reaction, the enzyme harnesses the substrate binding energy to create a distorted, ligand-depleted metal center, which serves to remove kinetic barriers to the production of the imidazolate intermediate. Subsequently, a second switch in coordination chemistry restores the octahedral coordination of the metal ion, leading to critical torsion angle changes to the substrate that are necessary for concomitant production of the diazafulvene
the manganese cluster is critical in converting the inactive trimeric state of the enzyme into its biologically active 24-mer and also forms the active site. The substrate is bound to the manganese cluster as an imidazole moiety that subsequently collapse to yield a diazafulvene intermediate
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crystallized in presence of Mn, unit-cell parameters: a = b = 157.9 A, c = 480 A, alpha = beta = 90°, gamma = 120°, with either 16 or 24 subunits in the asymmetric unit, space group R3, 3.0 A resolution
crystals belong to space group R3 with cell parameters a = 157.9 A, b = 157.9 A, c = 480 A, alpha = beta = 90°, gamma = 120°. Structure of manganese assembled, active form of the enzyme at 3.0 A resolution
structure of isoform IGPD2 in complex with phosphate, to 1.75 A resolution. The holoenzyme has an open conformation where the C-terminal region (R193-R206, termed the C loop), which contains a number of conserved residues, is disordered. structure of mutant E21Q, to 1.12 A resolution