5ER0
Water-forming NADH oxidase from Lactobacillus brevis (LbNOX)
Summary for 5ER0
| Entry DOI | 10.2210/pdb5er0/pdb |
| Descriptor | NADH oxidase, FLAVIN-ADENINE DINUCLEOTIDE, OXYGEN MOLECULE, ... (5 entities in total) |
| Functional Keywords | nadh oxidase, fad, molecular oxygen, oxidoreductase |
| Biological source | Lactobacillus brevis |
| Total number of polymer chains | 4 |
| Total formula weight | 228529.90 |
| Authors | Cracan, V.,Grabarek, Z. (deposition date: 2015-11-13, release date: 2016-04-13, Last modification date: 2023-09-27) |
| Primary citation | Titov, D.V.,Cracan, V.,Goodman, R.P.,Peng, J.,Grabarek, Z.,Mootha, V.K. Complementation of mitochondrial electron transport chain by manipulation of the NAD+/NADH ratio. Science, 352:231-235, 2016 Cited by PubMed Abstract: 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. PubMed: 27124460DOI: 10.1126/science.aad4017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.406 Å) |
Structure validation
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