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4oaq

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==Crystal structure of the R-specific Carbonyl Reductase from Candida parapsilosis ATCC 7330==
==Crystal structure of the R-specific Carbonyl Reductase from Candida parapsilosis ATCC 7330==
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<StructureSection load='4oaq' size='340' side='right' caption='[[4oaq]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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<StructureSection load='4oaq' size='340' side='right'caption='[[4oaq]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4oaq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OAQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4oaq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_parapsilosis Candida parapsilosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OAQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.858&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cinnamyl-alcohol_dehydrogenase Cinnamyl-alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.195 1.1.1.195] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oaq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oaq RCSB], [http://www.ebi.ac.uk/pdbsum/4oaq PDBsum]</span></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=4oaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oaq OCA], [https://pdbe.org/4oaq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oaq RCSB], [https://www.ebi.ac.uk/pdbsum/4oaq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oaq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/M4VRJ6_CANPA M4VRJ6_CANPA]
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The NAD(P)H-dependent carbonyl reductase from Candida parapsilosis ATCC 7330 catalyses the asymmetric reduction of ethyl 4-phenyl-2-oxobutanoate to ethyl (R)-4-phenyl-2-hydroxybutanoate, a precursor of angiotensin-converting enzyme inhibitors such as Cilazapril and Benazepril. The carbonyl reductase was expressed in Escherichia coli and purified by GST-affinity and size-exclusion chromatography. Crystals were obtained by the hanging-drop vapour-diffusion method and diffracted to 1.86 A resolution. The asymmetric unit contained two molecules of carbonyl reductase, with a solvent content of 48%. The structure was solved by molecular replacement using cinnamyl alcohol dehydrogenase from Saccharomyces cerevisiae as a search model.
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Expression, purification, crystallization and preliminary X-ray diffraction analysis of carbonyl reductase from Candida parapsilosis ATCC 7330.,Aggarwal N, Mandal PK, Gautham N, Chadha A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):313-5. doi:, 10.1107/S1744309113003667. Epub 2013 Feb 27. PMID:23519811<ref>PMID:23519811</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Carbonyl reductase 3D structures|Carbonyl reductase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cinnamyl-alcohol dehydrogenase]]
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[[Category: Candida parapsilosis]]
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[[Category: Aggrawal, N]]
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[[Category: Large Structures]]
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[[Category: Chadha, A]]
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[[Category: Aggrawal N]]
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[[Category: Gautham, N]]
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[[Category: Chadha A]]
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[[Category: Mandal, P K]]
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[[Category: Gautham N]]
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[[Category: Nadph]]
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[[Category: Mandal PK]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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[[Category: Stereoselectivity]]
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[[Category: Zinc dependent carbonyl reductase]]
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Current revision

Crystal structure of the R-specific Carbonyl Reductase from Candida parapsilosis ATCC 7330

PDB ID 4oaq

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