1hxh
COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE
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OverviewOverview
The enzyme 3beta/17beta-hydroxysteroid dehydrogenase (3beta/17beta-HSD) is, a steroid-inducible component of the Gram-negative bacterium Comamonas, testosteroni. It catalyzes the reversible reduction/dehydrogenation of the, oxo/beta-hydroxy groups at positions 3 and 17 of steroid compounds, including hormones and isobile acids. Crystallographic analysis at 1.2 A, resolution reveals the enzyme to have nearly identical subunits that form, a tetramer with 222 symmetry. This is one of the largest oligomeric, structures refined at this resolution. The subunit consists of a monomer, with a single-domain structure built around a seven-stranded beta-sheet, flanked by six alpha-helices. The active site contains a Ser-Tyr-Lys, triad, typical for short-chain dehydrogenases/reductases (SDR). Despite, their highly diverse substrate specificities, SDR members show a close to, identical folding pattern architectures and a common catalytic mechanism., In contrast to other SDR apostructures determined, the substrate binding, loop is well-defined. Analysis of structure-activity relationships of, catalytic cleft residues, docking analysis of substrates and inhibitors, and accessible surface analysis explains how 3beta/17beta-HSD accommodates, steroid substrates of different conformations.
About this StructureAbout this Structure
1HXH is a Single protein structure of sequence from Comamonas testosteroni. Active as 3(or 17)-beta-hydroxysteroid dehydrogenase, with EC number 1.1.1.51 Full crystallographic information is available from OCA.
ReferenceReference
Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition., Benach J, Filling C, Oppermann UC, Roversi P, Bricogne G, Berndt KD, Jornvall H, Ladenstein R, Biochemistry. 2002 Dec 17;41(50):14659-68. PMID:12475215
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