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Crystallographic studies on the binding of coenzyme analogs to D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor

Crystallographic studies on the binding of coenzyme analogs to D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor
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摘要 In contrast with the coezyme, two coenzyme analogs, ADP-ribose and SNAD, bind non-cooperatively to D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Palinurus versicolor (PV) GAPDH complexed with ADP-ribose and SNAD has been crystallized by the method of sitting-drop vapor diffusion. X-ray diffraction data analysis reveals that both crystals belong to the same space group (C2), and have similar cell dimensions: a =152.80 A, b =100.35 A, c =128.31 A, β=110.28° and a =153.41 A, b =100.51 A, c =128.44 A, β =110.48°, respectively. It is estimated that the asymmetric unit in each crystal contains 4 subunits. This is a novel crystal form which is quite different from that previously reported for holo- and apo-GAPDH from the same spurce. The result suggests that the binding of the two coenzyme analogs to GAPDH may lead to some significant conformational changes, which are different from those induced by the coenzyme binding. The self-rotation function indicates that the tetramer of these two GAPDH In contrast with the coezyme, two coenzyme analogs, ADP-ribose and SNAD, bind non-cooperatively to D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH).Palinurus versicolor (PV) GAPDH complexed with ADP-ribose and SNAD has been crystallized by the method of sitting-drop vapor diffusion. X-ray diffraction data analysis reveals that both crystals belong to the same space group (C2), and have similar cell dimensions: a =152.80 ?,b =100.35 ?, c =128.31 ?,β =110.28° and a =153.41 ?,b =100.51 ?,c =128.44 ?,β =110.48°, respectively. It is estimated that the asymmetric unit in each crystal contains 4 subunits. This is a novel crystal form which is quite different from that previously reported for holoand apo-GAPDH from the same source. The result suggests that the binding of the two coenzyme analogs to GAPDH may lead to some significant conformational changes, which are different from those induced by the coenzyme binding. The self-rotation function indicates that the tetramer of these two GAPDH complexes also has good 222 symmetry. The structural analysis and the comparison with holoand apo-GAPDH may give a clue to the cooperative mechanism of the enzyme.
机构地区 Chinese Acad Sci
出处 《Chinese Science Bulletin》 SCIE EI CAS 2000年第13期1199-1202,共4页
关键词 D-glyceraldehyde-3-phosphate DEHYDROGENASE ADP-RIBOSE SNAD crystal growth X-ray analysis. D-glyceraldehyde-3-phosphate dehydrogenase ADP-ribose SNAD crystal growth X-ray analysis
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