1hxh
From Proteopedia
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| - | | | + | {{STRUCTURE_1hxh| PDB=1hxh | SCENE= }} |
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'''COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE''' | '''COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE''' | ||
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==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/12475215 12475215] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12475215 12475215] | ||
| - | [[Category: 3(or 17)-beta-hydroxysteroid dehydrogenase]] | ||
[[Category: Comamonas testosteroni]] | [[Category: Comamonas testosteroni]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Oppermann, U C.T.]] | [[Category: Oppermann, U C.T.]] | ||
[[Category: Roversi, P.]] | [[Category: Roversi, P.]] | ||
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| - | [[Category: | + | [[Category: Rossmann fold]] |
| - | [[Category: | + | [[Category: Short-chain dehydrogenase]] |
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Revision as of 16:19, 2 May 2008
COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE
Overview
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 Structure
1HXH is a Single protein structure of sequence from Comamonas testosteroni. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 19:19:47 2008
