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| | <StructureSection load='2zat' size='340' side='right'caption='[[2zat]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='2zat' size='340' side='right'caption='[[2zat]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zat]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZAT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zat]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZAT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.5Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zat OCA], [http://pdbe.org/2zat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zat RCSB], [http://www.ebi.ac.uk/pdbsum/2zat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zat ProSAT]</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=2zat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zat OCA], [https://pdbe.org/2zat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zat RCSB], [https://www.ebi.ac.uk/pdbsum/2zat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zat ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DHRS4_PIG DHRS4_PIG]] Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones.<ref>PMID:12604222</ref> | + | [https://www.uniprot.org/uniprot/DHRS4_PIG DHRS4_PIG] Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones.<ref>PMID:12604222</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pig]] | + | [[Category: Sus scrofa]] |
| - | [[Category: Aoki, K]] | + | [[Category: Aoki K]] |
| - | [[Category: Nakamura, K T]] | + | [[Category: Nakamura KT]] |
| - | [[Category: Tanaka, N]] | + | [[Category: Tanaka N]] |
| - | [[Category: Alpha/beta]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
DHRS4_PIG Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Pig heart peroxisomal carbonyl reductase (PerCR) belongs to the short-chain dehydrogenase/reductase family, and its sequence comprises a C-terminal SRL tripeptide, which is a variant of the type 1 peroxisomal targeting signal (PTS1) Ser-Lys-Leu. PerCR is imported into peroxisomes of HeLa cells when the cells are transfected with vectors expressing the enzyme. However, PerCR does not show specific targeting when introduced into the cells with a protein transfection reagent. To understand the structural basis for peroxisomal localization of PerCR, we determined the crystal structure of PerCR. Our data revealed that the C-terminal PTS1 of each subunit of PerCR was involved in intersubunit interactions and was buried in the interior of the tetrameric molecule. These findings indicate that the PTS1 receptor Pex5p in the cytosol recognizes the monomeric form of PerCR whose C-terminal PTS1 is exposed, and that this PerCR is targeted into the peroxisome, thereby forming a tetramer.
Molecular basis for peroxisomal localization of tetrameric carbonyl reductase.,Tanaka N, Aoki K, Ishikura S, Nagano M, Imamura Y, Hara A, Nakamura KT Structure. 2008 Mar;16(3):388-97. PMID:18334214[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Usami N, Ishikura S, Abe H, Nagano M, Uebuchi M, Kuniyasu A, Otagiri M, Nakayama H, Imamura Y, Hara A. Cloning, expression and tissue distribution of a tetrameric form of pig carbonyl reductase. Chem Biol Interact. 2003 Feb 1;143-144:353-61. PMID:12604222
- ↑ Tanaka N, Aoki K, Ishikura S, Nagano M, Imamura Y, Hara A, Nakamura KT. Molecular basis for peroxisomal localization of tetrameric carbonyl reductase. Structure. 2008 Mar;16(3):388-97. PMID:18334214 doi:10.1016/j.str.2007.12.022
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