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| | ==Cytosolic Malate Dehydrogenase 1 (peroxide-treated)== | | ==Cytosolic Malate Dehydrogenase 1 (peroxide-treated)== |
| - | <StructureSection load='5nue' size='340' side='right' caption='[[5nue]], [[Resolution|resolution]] 1.35Å' scene=''> | + | <StructureSection load='5nue' size='340' side='right'caption='[[5nue]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nue]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NUE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NUE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nue]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NUE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ETX:2-ETHOXYETHANOL'>ETX</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.3500028Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ETX:2-ETHOXYETHANOL'>ETX</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nuf|5nuf]]</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=5nue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nue OCA], [https://pdbe.org/5nue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nue RCSB], [https://www.ebi.ac.uk/pdbsum/5nue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nue ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MDH1, At1g04410, F19P19.13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
| + | |
| - | <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>
| + | |
| - | <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=5nue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nue OCA], [http://pdbe.org/5nue PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nue RCSB], [http://www.ebi.ac.uk/pdbsum/5nue PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nue ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MDHC1_ARATH MDHC1_ARATH]] Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments.<ref>PMID:20876337</ref> | + | [https://www.uniprot.org/uniprot/MDHC1_ARATH MDHC1_ARATH] Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments.<ref>PMID:20876337</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5nue" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5nue" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Malate dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Huang, J]] | + | [[Category: Huang J]] |
| - | [[Category: Messens, J]] | + | [[Category: Messens J]] |
| - | [[Category: Reichheld, J P]] | + | [[Category: Reichheld J-P]] |
| - | [[Category: Young, D]] | + | [[Category: Young D]] |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Malate/oxaloacetate]]
| + | |
| - | [[Category: Nad+]]
| + | |
| - | [[Category: Oxidized]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
5nue is a 3 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.3500028Å |
| Ligands: | , , , , , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MDHC1_ARATH Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments.[1]
Publication Abstract from PubMed
Plant malate dehydrogenase (MDH) isoforms are found in different cell compartments and function in key metabolic pathways. It is well known that the chloroplastic NADP-dependent MDH activities are strictly redox regulated and controlled by light. However, redox dependence of other NAD-dependent MDH isoforms have been less studied. Here, we show by in vitro biochemical characterization that the major cytosolic MDH isoform (cytMDH1) is sensitive to H2O2 through sulfur oxidation of cysteines and methionines. CytMDH1 oxidation affects the kinetics, secondary structure, and thermodynamic stability of cytMDH1. Moreover, MS analyses and comparison of crystal structures between the reduced and H2O2-treated cytMDH1 further show that thioredoxin-reversible homodimerization of cytMDH1 through Cys330 disulfide formation protects the protein from overoxidation. Consistently, we found that cytosolic thioredoxins interact specifically with cytMDH in a yeast two-hybrid system. Importantly, we also show that cytosolic and chloroplastic, but not mitochondrial NAD-MDH activities are sensitive to H2O2 stress in Arabidopsis. NAD-MDH activities decreased both in a catalase2 mutant and in an NADP-thioredoxin reductase mutant, emphasizing the importance of the thioredoxin-reducing system to protect MDH from oxidation in vivo. We propose that the redox switch of the MDH activity contributes to adapt the cell metabolism to environmental constraints.
Self-protection of cytosolic malate dehydrogenase against oxidative stress in Arabidopsis.,Huang J, Niazi AK, Young D, Rosado LA, Vertommen D, Bodra N, Abdelgawwad MR, Vignols F, Wei B, Wahni K, Bashandy T, Bariat L, Van Breusegem F, Messens J, Reichheld JP J Exp Bot. 2017 Nov 29. pii: 4670922. doi: 10.1093/jxb/erx396. PMID:29194485[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tomaz T, Bagard M, Pracharoenwattana I, Linden P, Lee CP, Carroll AJ, Stroher E, Smith SM, Gardestrom P, Millar AH. Mitochondrial malate dehydrogenase lowers leaf respiration and alters photorespiration and plant growth in Arabidopsis. Plant Physiol. 2010 Nov;154(3):1143-57. doi: 10.1104/pp.110.161612. Epub 2010 Sep, 27. PMID:20876337 doi:http://dx.doi.org/10.1104/pp.110.161612
- ↑ Huang J, Niazi AK, Young D, Rosado LA, Vertommen D, Bodra N, Abdelgawwad MR, Vignols F, Wei B, Wahni K, Bashandy T, Bariat L, Van Breusegem F, Messens J, Reichheld JP. Self-protection of cytosolic malate dehydrogenase against oxidative stress in Arabidopsis. J Exp Bot. 2017 Nov 29. pii: 4670922. doi: 10.1093/jxb/erx396. PMID:29194485 doi:http://dx.doi.org/10.1093/jxb/erx396
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