CRYSTALLIZATION AND PRELIMINARY STRUCTURE OF PORCINE ALDEHYDE REDUCTASE NADPH BINARY COMPLEX

被引:2
|
作者
ELKABBANI, O
JUDGE, K
GINELL, SL
DELUCAS, LJ
FLYNN, TG
机构
[1] BROOKHAVEN NATL LAB, NATL SYNCHROTRON LIGHT SOURCE DEPT, ARGONNE NATL LAB, CTR STRUCT BIOL, UPTON, NY 11973 USA
[2] QUEENS UNIV, DEPT BIOCHEM, KINGSTON, ON K7L 3N6, CANADA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1995年 / 51卷
关键词
D O I
10.1107/S0907444994013995
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Porcine aldehyde reductase-NADPH binary complex has been crystallized from a buffered ammonium sulfate solution. The crystal form is hexagonal, space group P6(5)22, with a = b = 67.2, c = 243.7 Angstrom, alpha = beta = 90.0 and gamma = 120.0 degrees. A molecular-replacement structure solution has been successfully obtained by using the refined structure of the apoenzyme as the search model. The crystallographic R factor is currently equal to 0.24 after energy minimization using data between 8 and 3.0 Angstrom resolution. The aldehyde reductase-NADPH complex model is supported by electron density corresponding to NADPH not included in the search model. The tertiary structure of aldehyde reductase consists of a beta/alpha-barrel with the coenzyme-binding site located at the carboxy-terminal end of the strands of the barrel. The structure of aldehyde reductase-NADPH binary complex will help clarify the mechanism of action for this enzyme and will lead to the development of pharmacologic agents to delay or prevent diabetic complications.
引用
收藏
页码:605 / 608
页数:4
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