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| | ==Crystal structure of NADPH bound carbonyl reductase from chicken fatty liver== | | ==Crystal structure of NADPH bound carbonyl reductase from chicken fatty liver== |
| - | <StructureSection load='3wxb' size='340' side='right' caption='[[3wxb]], [[Resolution|resolution]] 1.98Å' scene=''> | + | <StructureSection load='3wxb' size='340' side='right'caption='[[3wxb]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wxb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WXB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WXB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wxb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WXB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LOC415661 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonyl_reductase_(NADPH) Carbonyl reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.184 1.1.1.184] </span></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=3wxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wxb OCA], [https://pdbe.org/3wxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wxb RCSB], [https://www.ebi.ac.uk/pdbsum/3wxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wxb ProSAT]</span></td></tr> |
| - | <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=3wxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wxb OCA], [http://pdbe.org/3wxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wxb RCSB], [http://www.ebi.ac.uk/pdbsum/3wxb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wxb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F1N9C1_CHICK F1N9C1_CHICK] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Araki, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Fukuda, Y]] | + | [[Category: Araki T]] |
| - | [[Category: Ohshima, T]] | + | [[Category: Fukuda Y]] |
| - | [[Category: Sakuraba, H]] | + | [[Category: Ohshima T]] |
| - | [[Category: Sone, T]] | + | [[Category: Sakuraba H]] |
| - | [[Category: Yoneda, K]] | + | [[Category: Sone T]] |
| - | [[Category: Carbonyl reductase]]
| + | [[Category: Yoneda K]] |
| - | [[Category: Chicken fatty liver]]
| + | |
| - | [[Category: Dehydrogenase/reductase]]
| + | |
| - | [[Category: Oxidoreductase activator]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
F1N9C1_CHICK
Publication Abstract from PubMed
A gene encoding a functionally unknown protein that is specifically expressed in the thyroidectomized chicken fatty liver and has a predicted amino acid sequence similar to that of NAD(P)H-dependent carbonyl reductase was overexpressed in Escherichia coli; its product was purified and characterized. The expressed enzyme was an NAD(P)H-dependent broad substrate specificity carbonyl reductase and was inhibited by arachidonic acid at 1.5 mum. Enzymological characterization indicated that the enzyme could be classified as a cytosolic-type carbonyl reductase. The enzyme's 3D structure was determined using the molecular replacement method at 1.98 A resolution in the presence of NADPH and ethylene glycol. The asymmetric unit consisted of two subunits, and a noncrystallographic twofold axis generated the functional dimer. The structures of the subunits, A and B, differed from each other. In subunit A, the active site contained an ethylene glycol molecule absent in subunit B. Consequently, Tyr172 in subunit A rotated by 103.7 degrees in comparison with subunit B, which leads to active site closure in subunit A. In Y172A mutant, the Km value for 9,10-phenanthrenequinone (model substrate) was 12.5 times higher than that for the wild-type enzyme, indicating that Tyr172 plays a key role in substrate binding in this carbonyl reductase. Because the Tyr172-containing active site lid structure (Ile164-Gln174) is not conserved in all known carbonyl reductases, our results provide new insights into substrate binding of carbonyl reductase. The catalytic properties and crystal structure revealed that thyroidectomized chicken fatty liver carbonyl reductase is a novel enzyme.
A novel NAD(P)H-dependent carbonyl reductase specifically expressed in the thyroidectomized chicken fatty liver: catalytic properties and crystal structure.,Fukuda Y, Sone T, Sakuraba H, Araki T, Ohshima T, Shibata T, Yoneda K FEBS J. 2015 Oct;282(20):3918-28. doi: 10.1111/febs.13385. Epub 2015 Aug 14. PMID:26206323[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fukuda Y, Sone T, Sakuraba H, Araki T, Ohshima T, Shibata T, Yoneda K. A novel NAD(P)H-dependent carbonyl reductase specifically expressed in the thyroidectomized chicken fatty liver: catalytic properties and crystal structure. FEBS J. 2015 Oct;282(20):3918-28. doi: 10.1111/febs.13385. Epub 2015 Aug 14. PMID:26206323 doi:http://dx.doi.org/10.1111/febs.13385
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