1hxh
From Proteopedia
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| - | [[Image:1hxh.gif|left|200px]] | + | [[Image:1hxh.gif|left|200px]] |
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| - | '''COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE''' | + | {{Structure |
| + | |PDB= 1hxh |SIZE=350|CAPTION= <scene name='initialview01'>1hxh</scene>, resolution 1.22Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/3(or_17)-beta-hydroxysteroid_dehydrogenase 3(or 17)-beta-hydroxysteroid dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.51 1.1.1.51] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HXH is a [ | + | 1HXH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXH OCA]. |
==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:// | + | 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: 3(or 17)-beta-hydroxysteroid dehydrogenase]] | ||
[[Category: Comamonas testosteroni]] | [[Category: Comamonas testosteroni]] | ||
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[[Category: short-chain dehydrogenase]] | [[Category: short-chain dehydrogenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:42:50 2008'' |
Revision as of 09:42, 20 March 2008
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| , resolution 1.22Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | 3(or 17)-beta-hydroxysteroid dehydrogenase, with EC number 1.1.1.51 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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