Crystallization and structural analysis of GADPH from Spinacia oleracea in a new form.
Two crystalline forms of GADPH (D-glyceraldehyde-3-phosphate dehydrogenase) from Spinacia oleracea were obtained using sitting-drop vapor diffusion. Despite the very low concentration of GADPH in the solutions, two crystalline forms were obtained, one of which was the previously reported C222 space group with unit-cell parameters a = 155.3, b = 181.7, c = 107.6 A and the other of which belonged to a new space group I4(1)22, with unit-cell parameters a = b = 120.9, c = 154.5 A. Diffraction data were measured from both native and derivatives, yielding structures at a resolution limit of 3.0 A. Differences at the NAD(+)/NADP(+)-binding site seen in these structures compared with the previously reported structure with bound coenzyme suggest that conformational changes associated with pyridine-nucleotide binding may play a role in the regulation of this enzyme.
Cámara-Artigas
Ana
A
Departamento Química-Física, Bioquímica y Química Inorgánica, Universidad de Almería, Carretera Sacramento, Almería 04120, Spain.
Hirasawa
Masakazu
M
Knaff
David B
DB
Wang
Meitian
M
Allen
James P
JP
D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D024601:Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D009249:NADP / Q000737:chemistry / Q000378:metabolism; D018515:Plant Leaves / Q000201:enzymology; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification; D011487:Protein Conformation; D018724:Spinacia oleracea / Q000201:enzymology*; D014961:X-Ray Diffraction
D010940:Plant Proteins; D009249:NADP; D024601:Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)