4gac

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==High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form==
==High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form==
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<StructureSection load='4gac' size='340' side='right' caption='[[4gac]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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<StructureSection load='4gac' size='340' side='right'caption='[[4gac]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gac]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GAC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GAC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gac]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GAC 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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]] 1.64&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Akr1a1, Akr1a4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></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/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </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=4gac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gac OCA], [https://pdbe.org/4gac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gac RCSB], [https://www.ebi.ac.uk/pdbsum/4gac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gac ProSAT]</span></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=4gac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gac OCA], [http://pdbe.org/4gac PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gac RCSB], [http://www.ebi.ac.uk/pdbsum/4gac PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gac ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AK1A1_MOUSE AK1A1_MOUSE]] Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity).
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[https://www.uniprot.org/uniprot/AK1A1_MOUSE AK1A1_MOUSE] Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Aldo-keto reductase 1a4 (AKR1a4; EC 1.1.1.2) is the mouse orthologue of human aldehyde reductase (AKR1a1), the founding member of the AKR family. As an NADPH-dependent enzyme, AKR1a4 catalyses the conversion of D-glucuronate to L-gulonate. AKR1a4 is involved in ascorbate biosynthesis in mice, but has also recently been found to interact with SMAR1, providing a novel mechanism of ROS regulation by ATM. Here, the crystal structure of AKR1a4 in its apo form at 1.64 A resolution as well as the characterization of the binding of AKR1a4 to NADPH and P44, a peptide derived from SMAR1, is presented.
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High-resolution structure of AKR1a4 in the apo form and its interaction with ligands.,Faucher F, Jia Z Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1271-4., doi: 10.1107/S1744309112037128. Epub 2012 Oct 26. PMID:23143230<ref>PMID:23143230</ref>
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==See Also==
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
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</div>
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<div class="pdbe-citations 4gac" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Faucher, F]]
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[[Category: Mus musculus]]
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[[Category: Jia, Z]]
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[[Category: Faucher F]]
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[[Category: Aldheyde reductase akr1a4]]
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[[Category: Jia Z]]
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[[Category: Oxidoreductase]]
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[[Category: Smar1]]
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[[Category: Tim barrel]]
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Current revision

High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form

PDB ID 4gac

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