1fjh: Difference between revisions

Revision as of 13:39, 21 February 2008

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. Active as 3-alpha-hydroxysteroid dehydrogenase (B-specific), with EC number 1.1.1.50 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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-[[Image:1fjh.jpg|left|200px]]<br /><applet load="1fjh" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1fjh, resolution 1.68&Aring;" />
 '''THE CRYSTAL STRUCTURE OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY'''<br />
 ==Overview==
-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.
+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 Structure==
-FJH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FJH OCA].
+FJH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJH OCA].
 ==Reference==
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 [[Category: xenobiotic]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:55:24 2007''
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