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| | {{STRUCTURE_1ral| PDB=1ral | SCENE= }} | | {{STRUCTURE_1ral| PDB=1ral | SCENE= }} |
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| - | '''THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE SUPERFAMILY'''
| + | ===THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE SUPERFAMILY=== |
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| - | ==Overview==
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| - | The 3.0-A-resolution x-ray structure of rat liver 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase (3 alpha-HSD, EC 1.1.1.50) was determined by molecular replacement using human placental aldose reductase as the search model. The protein folds into an alpha/beta or triose-phosphate isomerase barrel and lacks a canonical Rossmann fold for binding pyridine nucleotide. The structure contains a concentration of hydrophobic amino acids that lie in a cavity near the top of the barrel and that are presumed to be involved in binding hydrophobic substrates (steroids, prostaglandins, and polycyclic aromatic hydrocarbons) and inhibitors (nonsteroidal antiinflammatory drugs). At the distal end of this cavity lie three residues in close proximity that have been implicated in catalysis by site-directed mutagenesis--Tyr-55, Asp-50, and Lys-84. Tyr-55 is postulated to act as the general acid. 3 alpha-HSD shares significant sequence identity with other HSDs that belong to the aldo-keto reductase superfamily and these may show similar architecture. Other members of this family include prostaglandin F synthase and rho-crystallin. By contrast, 3 alpha-HSD shares no sequence identity with HSDs that are members of the short-chain alcohol dehydrogenase family but does contain the Tyr-Xaa-Xaa-Xaa-Lys consensus sequence implicated in catalysis in this family. In the 3 alpha-HSD structure these residues are on the periphery of the barrel and are unlikely to participate in catalysis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8146147}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8146147 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8146147}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Penning, T M.]] | | [[Category: Penning, T M.]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:16:39 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:23:32 2008'' |
Revision as of 23:23, 27 July 2008
Template:STRUCTURE 1ral
THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE SUPERFAMILY
Template:ABSTRACT PUBMED 8146147
About this Structure
1RAL is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily., Hoog SS, Pawlowski JE, Alzari PM, Penning TM, Lewis M, Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2517-21. PMID:8146147
Page seeded by OCA on Mon Jul 28 02:23:32 2008
