5er0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Water-forming NADH oxidase from Lactobacillus brevis (LbNOX)== | |
| + | <StructureSection load='5er0' size='340' side='right'caption='[[5er0]], [[Resolution|resolution]] 2.41Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5er0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Levilactobacillus_brevis Levilactobacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ER0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ER0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.406Å</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></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=5er0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5er0 OCA], [https://pdbe.org/5er0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5er0 RCSB], [https://www.ebi.ac.uk/pdbsum/5er0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5er0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q03Q85_LEVBA Q03Q85_LEVBA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A decline in electron transport chain (ETC) activity is associated with many human diseases. Although diminished mitochondrial adenosine triphosphate production is recognized as a source of pathology, the contribution of the associated reduction in the ratio of the amount of oxidized nicotinamide adenine dinucleotide (NAD(+)) to that of its reduced form (NADH) is less clear. We used a water-forming NADH oxidase from Lactobacillus brevis (LbNOX) as a genetic tool for inducing a compartment-specific increase of the NAD(+)/NADH ratio in human cells. We used LbNOX to demonstrate the dependence of key metabolic fluxes, gluconeogenesis, and signaling on the cytosolic or mitochondrial NAD(+)/NADH ratios. Expression of LbNOX in the cytosol or mitochondria ameliorated proliferative and metabolic defects caused by an impaired ETC. The results underscore the role of reductive stress in mitochondrial pathogenesis and demonstrate the utility of targeted LbNOX for direct, compartment-specific manipulation of redox state. | ||
| - | + | Complementation of mitochondrial electron transport chain by manipulation of the NAD+/NADH ratio.,Titov DV, Cracan V, Goodman RP, Peng J, Grabarek Z, Mootha VK Science. 2016 Apr 8;352(6282):231-5. doi: 10.1126/science.aad4017. Epub 2016 Apr , 7. PMID:27124460<ref>PMID:27124460</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Cracan | + | <div class="pdbe-citations 5er0" style="background-color:#fffaf0;"></div> |
| - | [[Category: Grabarek | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Levilactobacillus brevis]] | ||
| + | [[Category: Cracan V]] | ||
| + | [[Category: Grabarek Z]] | ||
Current revision
Water-forming NADH oxidase from Lactobacillus brevis (LbNOX)
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