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

被引:3
|
作者
Shen, YQ [1 ]
Song, SY [1 ]
Lin, ZJ [1 ]
机构
[1] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
来源
关键词
D-glyceraldehyde-3-phosphate dehydrogenase; allosteric enzyme and crystal structure;
D O I
10.1007/BF02881723
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
D-glyceraldehyde-3-phosphate dehydrogenase (holo-GAPDH) from Palinurus versicolor was crystallized in a novel crystal form by the method of sitting-drop vapor diffusion. The crystals have space group P42(1)2, 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 crystallographic R-free and R factors of 0.274 and 0.262, and r.m.s. deviations of 0.002 nm for bond lengths and 2.33 degrees 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:9
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