5voh | pdb_00005voh

Crystal structure of engineered water-forming NADPH oxidase (TPNOX) bound to NADPH. The G159A, D177A, A178R, M179S, P184R mutant of LbNOX.

spinqualitylabelsall models 5voh, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5voh is a 4 chain structure with sequence from Levilactobacillus brevis KB290. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.302Å Ligands: CL, CSO, EDO, FAD, NDP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M5B0V2_LEVBR Publication Abstract from PubMed 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 H2O-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. A genetically encoded tool for manipulation of NADP+/NADPH in living cells.,Cracan V, Titov DV, Shen H, Grabarek Z, Mootha VK Nat Chem Biol. 2017 Aug 7. doi: 10.1038/nchembio.2454. PMID:28805804 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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