Structure of D-glyceraldehyde-3-phosphate dehydrogenase fromPalinurus versicolor in a tetragonal crystal form

被引:0
作者
Yuequan Shen
Shiying Song
Zhengjiong Lin
机构
[1] Chinese Academy of Sciences,National Laboratory of Biomacromolecules, Institute of Biophysics
来源
Science in China Series C: Life Sciences | 2000年 / 43卷
关键词
D-glyceraldehyde-3-phosphate dehydrogenase; allosteric enzyme and crystal structure;
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摘要
D-glyceraldehyde-3-phosphate dehydrogenase (holo-GAPDH) fromPalinurus versicolor was crystallized in a novel crystal form by the method of sitting-drop vapor diffusion. The crystals have space groupP4212, cell parameters a=15.49 nm, c=8.03 nm and two subunits per asymmetric unit. The crystal structure at 0.34 nm was determined by the molecular replacement method. The final model has crystallographicRfree andR factors of 0.274 and 0.262, and r.m.s. deviations of 0.002 nm for bond lengths and 2.33° for bond angles. The two subunits in asymmetric unit are similar to each other not only in the three-dimensional structure, but also in average temperature factors. This result demonstrates that the obvious difference in average temperature factors for the different subunits in C2 crystal form reported previously may be attributed to the different crystallographic environments of the subunits. This further supports that holo-GAPDH has a good 222 molecular symmetry.
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页码:96 / 104
页数:8
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