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  • Title: Purification, crystallization and preliminary X-ray diffraction results of human 17beta-hydroxysteroid dehydrogenase type 5.
    Author: Zhou M, Qiu W, Chang HJ, Gangloff A, Lin SX.
    Journal: Acta Crystallogr D Biol Crystallogr; 2002 Jun; 58(Pt 6 Pt 2):1048-50. PubMed ID: 12037313.
    Abstract:
    17beta-Hydroxysteroid dehydrogenases (17beta-HSDs) catalyze the last step in the biosynthesis of all androgens and estrogens, thus playing a pivotal role in sex-hormone metabolism. Human 17beta-HSD type 5 (17beta-HSD5) catalyzes hydride transfer at the 17beta-hydroxy position, but possesses high sequence homology to 3alpha-hydroxysteroid dehydrogenases (3alpha-HSD). Two crystal forms of 17beta-HSD5 in an enzyme-testosterone-NADP ternary complex have been obtained under different crystallization conditions. A form I crystal obtained at pH 8.5 diffracted to 1.32 A. It belonged to space group P2(1), with unit-cell parameters a = 47.41, b = 77.16, c = 48.67 A, beta = 116.32 degrees. Form II crystals obtained at pH 6.5 diffracted to 2.0 A and belonged to space group P6(3), with unit-cell parameters a = b = 110.58, c = 56.89 A.
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