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Crystallization (Commentary)
AGPR apoenzyme and AGPR in complex with NADP+ crystallized by the sitting-drop method. Crystals of the apoenzyme belong to space group P212121 with four protein subunits in the asymmetric unit (a crystallographic tetramer) and to space group C2 having two protein subunits in the asymmetric unit (a crystallographic C2-dimer). Each AGPR subunit consists of alpha/beta and alpha + beta domains. NADP+ is bound in the cleft between them. Conformational change in AGPR upon NADP+ binding, a loop (Leu88 to His92) moves more than 5 A to confine sterically the cofactor's adenine moiety in a hydrophobic pocket. Residues His217 and His219 can form hydrogen bonds with the docked substrate. An ion pair can form between the substrate phosphate group and the guanidinium group of Arg114, which optimally places and orients the substrate for subsequent nucleophilic attack by Cys158 on the substrate gamma-carboxyl group
hanging-drop vapour-diffusion method using PEG 4000 as a precipitating agent, colourless prosms, with unit-cell parameters a = b = 90.0 A, c = 139.5 A. The crystals belong to the hexagonal space group P6(2)22 or P6(4)22
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