1fjh: Difference between revisions
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[[Image:1fjh.jpg|left|200px]] | [[Image:1fjh.jpg|left|200px]] | ||
'''THE CRYSTAL STRUCTURE OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY''' | {{Structure | ||
|PDB= 1fjh |SIZE=350|CAPTION= <scene name='initialview01'>1fjh</scene>, resolution 1.68Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/3-alpha-hydroxysteroid_dehydrogenase_(B-specific) 3-alpha-hydroxysteroid dehydrogenase (B-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.50 1.1.1.50] | |||
|GENE= | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FJH is a [ | 1FJH 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=1FJH OCA]. | ||
==Reference== | ==Reference== | ||
The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family., Grimm C, Maser E, Mobus E, Klebe G, Reuter K, Ficner R, J Biol Chem. 2000 Dec 29;275(52):41333-9. PMID:[http:// | The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family., Grimm C, Maser E, Mobus E, Klebe G, Reuter K, Ficner R, J Biol Chem. 2000 Dec 29;275(52):41333-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11007791 11007791] | ||
[[Category: 3-alpha-hydroxysteroid dehydrogenase (B-specific)]] | [[Category: 3-alpha-hydroxysteroid dehydrogenase (B-specific)]] | ||
[[Category: Comamonas testosteroni]] | [[Category: Comamonas testosteroni]] | ||
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[[Category: xenobiotic]] | [[Category: xenobiotic]] | ||
''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 11:10:00 2008'' | ||
Revision as of 12:10, 20 March 2008
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| , resolution 1.68Å | |||||||
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| Activity: | 3-alpha-hydroxysteroid dehydrogenase (B-specific), with EC number 1.1.1.50 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY
OverviewOverview
The crystal structure of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni (3alpha-HSDH) as well as the structure of its binary complex with NAD(+) have been solved at 1.68-A and 1.95-A resolution, respectively. The enzyme is a member of the short chain dehydrogenase/reductase (SDR) family. Accordingly, the active center and the conformation of the bound nucleotide cofactor closely resemble those of other SDRs. The crystal structure reveals one homodimer per asymmetric unit representing the physiologically active unity. Dimerization takes place via an interface essentially built-up by helix alphaG and strand betaG of each subunit. So far this type of intermolecular contact has exclusively been observed in homotetrameric SDRs but never in the structure of a homodimeric SDR. The formation of a tetramer is blocked in 3alpha-HSDH by the presence of a predominantly alpha-helical subdomain which is missing in all other SDRs of known structure.
About this StructureAbout this Structure
1FJH is a Single protein structure of sequence from Comamonas testosteroni. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family., Grimm C, Maser E, Mobus E, Klebe G, Reuter K, Ficner R, J Biol Chem. 2000 Dec 29;275(52):41333-9. PMID:11007791
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