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1ral

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(New page: 200px<br /><applet load="1ral" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ral, resolution 3.&Aring;" /> '''THREE-DIMENSIONAL STRU...)
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[[Image:1ral.jpg|left|200px]]<br /><applet load="1ral" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ral, resolution 3.&Aring;" />
 
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'''THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE SUPERFAMILY'''<br />
 
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==Overview==
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==THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE SUPERFAMILY==
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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.
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<StructureSection load='1ral' size='340' side='right'caption='[[1ral]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ral]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RAL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ral FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ral OCA], [https://pdbe.org/1ral PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ral RCSB], [https://www.ebi.ac.uk/pdbsum/1ral PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ral ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DIDH_RAT DIDH_RAT] Besides being a 3-alpha-hydroxysteroid dehydrogenase, the enzyme can accomplish diverse functions: as quinone reductase, as an aromatic alcohol dehydrogenase, as dihydrodiol dehydrogenase, and as 9-, 11-, and 15-hydroxyprostaglandin dehydrogenase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ra/1ral_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ral ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1RAL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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=1RAL OCA].
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*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8146147 8146147]
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[[Category: Large Structures]]
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[[Category: 3-alpha-hydroxysteroid dehydrogenase (B-specific)]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Alzari PM]]
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[[Category: Alzari, P.M.]]
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[[Category: Hoog SS]]
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[[Category: Hoog, S.S.]]
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[[Category: Lewis M]]
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[[Category: Lewis, M.]]
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[[Category: Pawlowski JE]]
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[[Category: Pawlowski, J.E.]]
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[[Category: Penning TM]]
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[[Category: Penning, T.M.]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:24:34 2007''
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Current revision

THREE-DIMENSIONAL STRUCTURE OF RAT LIVER 3ALPHA-HYDROXYSTEROID(SLASH)DIHYDRODIOL DEHYDROGENASE: A MEMBER OF THE ALDO-KETO REDUCTASE SUPERFAMILY

PDB ID 1ral

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