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1.1.1.209: 3(or 17)alpha-hydroxysteroid dehydrogenase

This is an abbreviated version!
For detailed information about 3(or 17)alpha-hydroxysteroid dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.209

Reaction

androsterone
+
NAD(P)+
=
5alpha-androstane-3,17-dione
 +
NAD(P)H
 +
H+

Synonyms

3(17)alpha-hydroxysteroid dehydrogenase, 3beta- and 17beta-hydroxysteroid dehydrogenase, AKR1C21, dehydrogenase, 3(17)alpha-hydroxy steroid, More

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.209 3(or 17)alpha-hydroxysteroid dehydrogenase

Crystallization

Crystallization on EC 1.1.1.209 - 3(or 17)alpha-hydroxysteroid dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
double mutant G225P/G226P of AKR1C21 in complex with the coenzyme NADP+ and the inhibitor hexoestrol, by hanging-drop vapour-diffusion method, at 2.1 A resolution. Overall fold of the mutant is similar to that of wild-type, apart from the loop region lining the active-site pocket, in which the two glycines at positions 225 and 226 are mutated to prolines which have a more rigid structure, resulting in a larger substrate-binding pocket. The mutation affects the conformation of the adjoining residues Tyr224 and Trp227, resulting in a further opening up of the active-site pocket while the catalytic residues remain unaffected. The inhibitor molecule is bound to the active site with one hydroxyl group pointing towards the catalytic residues, the bulky phenyl rings and the methyl groups of hexoestrol form van der Waals contacts with Trp227, Tyr224, Tyr55 and the nicotinamide ring of NADP+
purified recombinant enzyme, in a AKR1C21-NADPH binary complex, hanging drop vapour diffusion method, 22°C, 18 mg/ml of protein in 0.1 M HEPES, pH 7.5, 10% PEG 6000, and 5% 2-methyl-2,4-pentanediol, mixing with an equal volume of the crystallization buffer, and equilibration against 1 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.8 A resolution
purified recombinant isozyme AKR1C21, hanging drop vapour diffusion method, 16 mg/ml enzyme in 10 mM Tris-HCl, pH 7.5, and 2 mM 2-mercaptoethanol, mixed with an equal volume of 0.003 ml of reservoir solution containing 0.1 M HEPES, pH 7.5, 10% PEG 6000, 5% 2-methyl-2,4-pentanediol, equilibration against 1 ml reservoir solution, 22°C, 1 week, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement
-
Y224D mutant at 2.3 A resolution. Mutation results in a change in the conformation of the flexible loop B, including the V-shaped groove