5zi4

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'''Unreleased structure'''
 
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The entry 5zi4 is ON HOLD until Paper Publication
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==MDH3 wild type, nad-oaa-form==
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<StructureSection load='5zi4' size='340' side='right' caption='[[5zi4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5zi4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZI4 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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</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/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </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=5zi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zi4 OCA], [http://pdbe.org/5zi4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zi4 RCSB], [http://www.ebi.ac.uk/pdbsum/5zi4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zi4 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Malate dehydrogenase (MDH), a carbohydrate and energy metabolism enzyme in eukaryotes, catalyzes the interconversion of malate to oxaloacetate (OAA) in conjunction with that of nicotinamide adenine dinucleotide (NAD(+)) to NADH. Three isozymes of MDH have been reported in Saccharomyces cerevisiae: MDH1, MDH2 and MDH3. MDH1 is a mitochondrial enzyme and a member of the tricarboxylic acid cycle, whereas MDH2 is a cytosolic enzyme that functions in the glyoxylate cycle. MDH3 is a glyoxysomal enzyme that is involved in the reoxidation of NADH, which is produced during fatty-acid beta-oxidation. The affinity of MDH3 for OAA is lower than those of MDH1 and MDH2. Here, the crystal structures of yeast apo MDH3, the MDH3-NAD(+) complex and the MDH3-NAD(+)-OAA ternary complex were determined. The structure of the ternary complex suggests that the active-site loop is in the open conformation, differing from the closed conformations in mitochondrial and cytosolic malate dehydrogenases.
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Authors:
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Structure of glyoxysomal malate dehydrogenase (MDH3) from Saccharomyces cerevisiae.,Moriyama S, Nishio K, Mizushima T Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):617-624. doi:, 10.1107/S2053230X18011895. Epub 2018 Sep 19. PMID:30279312<ref>PMID:30279312</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5zi4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Malate dehydrogenase]]
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[[Category: Mizushima, T]]
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[[Category: Moriyama, S]]
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[[Category: Nishio, K]]
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[[Category: Fatty acid oxidation]]
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[[Category: Glyoxysome]]
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[[Category: Mdh3]]
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[[Category: Oxidoreductase]]

Revision as of 05:48, 24 October 2018

MDH3 wild type, nad-oaa-form

5zi4, resolution 2.10Å

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