5VN0
Water-forming NADH oxidase from Lactobacillus brevis (LbNOX) bound to NADH.
Summary for 5VN0
| Entry DOI | 10.2210/pdb5vn0/pdb |
| Related | 5VOH |
| Descriptor | NAD(FAD)-dependent dehydrogenase, FLAVIN-ADENINE DINUCLEOTIDE, OXYGEN MOLECULE, ... (6 entities in total) |
| Functional Keywords | substrate bound, redox active cysteine, water-forming oxidase, oxidoreductase |
| Biological source | Lactobacillus brevis (strain ATCC 367 / JCM 1170) |
| Total number of polymer chains | 8 |
| Total formula weight | 461700.59 |
| Authors | Cracan, V.,Grabarek, Z. (deposition date: 2017-04-28, release date: 2017-08-02, Last modification date: 2023-10-04) |
| Primary citation | Cracan, V.,Titov, D.V.,Shen, H.,Grabarek, Z.,Mootha, V.K. A genetically encoded tool for manipulation of NADP(+)/NADPH in living cells. Nat. Chem. Biol., 13:1088-1095, 2017 Cited by PubMed Abstract: The redox coenzymes NADH and NADPH are broadly required for energy metabolism, biosynthesis and detoxification. Despite detailed knowledge of specific enzymes and pathways that utilize these coenzymes, a holistic understanding of the regulation and compartmentalization of NADH- and NADPH-dependent pathways is lacking, partly because of a lack of tools with which to investigate these processes in living cells. We have previously reported the use of the naturally occurring Lactobacillus brevis HO-forming NADH oxidase (LbNOX) as a genetic tool for manipulation of the NAD/NADH ratio in human cells. Here, we present triphosphopyridine nucleotide oxidase (TPNOX), a rationally designed and engineered mutant of LbNOX that is strictly specific to NADPH. We characterized the effects of TPNOX expression on cellular metabolism and used it in combination with LbNOX to show how the redox states of mitochondrial NADPH and NADH pools are connected. PubMed: 28805804DOI: 10.1038/nchembio.2454 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.001 Å) |
Structure validation
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