1n5d: Difference between revisions

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-[[Image:1n5d.gif|left|200px]]<br /><applet load="1n5d" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1n5d, resolution 2.30&Aring;" />
-'''CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE==
-Porcine testicular carbonyl reductase (PTCR) belongs to the short chain, dehydrogenases/reductases (SDR) superfamily and catalyzes the, NADPH-dependent reduction of ketones on steroids and prostaglandins. The, enzyme shares nearly 85% sequence identity with the NADPH-dependent human, 15-hydroxyprostaglandin dehydrogenase/carbonyl reductase. The tertiary, structure of the enzyme at 2.3 A reveals a fold characteristic of the SDR, superfamily that uses a Tyr-Lys-Ser triad as catalytic residues, but, exhibits neither the functional homotetramer nor the homodimer that, distinguish all SDRs. It is the first known monomeric structure in the SDR, superfamily. In PTCR, which is also active as a monomer, a 41-residue, insertion immediately before the catalytic Tyr describes an all-helix, subdomain that packs against interfacial helices, eliminating the, four-helix bundle interface conserved in the superfamily. An additional, anti-parallel strand in the PTCR structure also blocks the other, strand-mediated interface. These novel structural features provide the, basis for the scaffolding of one catalytic site within a single molecule, of the enzyme.
+<StructureSection load='1n5d' size='340' side='right'caption='[[1n5d]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1n5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hu4 1hu4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N5D FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n5d OCA], [https://pdbe.org/1n5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n5d RCSB], [https://www.ebi.ac.uk/pdbsum/1n5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n5d ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CBR1_PIG CBR1_PIG] NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione (By similarity).<ref>PMID:1377683</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/1n5d_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1n5d ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-N5D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with SO4 and NDP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1HU4. Active as [http://en.wikipedia.org/wiki/3-alpha-(or_20-beta)-hydroxysteroid_dehydrogenase 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.53 1.1.1.53] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N5D OCA].
+*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
+== References ==
-==Reference==
+<references/>
-Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases., Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, Duax WL, J Biol Chem. 2001 May 25;276(21):18457-63. Epub 2001 Mar 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11279087 11279087]
+__TOC__
-[[Category: 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase]]
+</StructureSection>
-[[Category: Single protein]]
+[[Category: Large Structures]]
 [[Category: Sus scrofa]]
-[[Category: Ghosh, D.]]
+[[Category: Ghosh D]]
-[[Category: NDP]]
-[[Category: SO4]]
-[[Category: monomer]]
-[[Category: nadp-complex]]
-[[Category: shortchain dehydrogenase/reductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:58:33 2007''