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Higher plants have two distinct glyceraldehyde-3-phosphate dehydrogenases (GAPDHs): cytosolic NAD-GAPDH and chloroplastic NADP-GAPDH. The cytosolic enzyme requires NAD as the sole coenzyme, while the chloroplastic enzyme utilizes both NADP(H) and NAD(H). The cyano bacterium Synechococcus PCC 7942 possesses only NADP-GAPDH as a tetramer. This NADP-GAPDH is not greatly activated by light irradiation or by addition of NADPH, being different from those of higher plants. We have determined the crystal structure of NADP-GAPDH originated from S. 7942 to elucidate the structure-function relationships of GAPDHs and to obtain some information about the activation mechanism. The recombinant NADP-GAPDH was expressed in Escherichia coli and the purified enzyme was crystallized using ammonium sulfate as a precipitant. The crystals were also soaked with NADP for 3 days. A complete data set was collected to a resolution of 2.5 Å using synchrotron radiation at KEK-PF. The crystals belonged to the monoclinic space group C2 with unit-cell parameters a = 149.4, b = 79.3 and c = 427.8 Å , and β = 101.3° . The structure was solved by the molecular replacement method. The electron density maps revealed the position of the cofactor in each subunit. Assignment of NADP improved the model to an R-factor of 20.7% with an R-free of 26.4%. The crystal structure revealed that one of a pair of Cys residues, both of which are involved in the light/dark regulation of the chloroplastic enzyme, is not found in the present enzyme.

Crystal structure of the NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of cyanobacteria