5VN0

Water-forming NADH oxidase from Lactobacillus brevis (LbNOX) bound to NADH.

5VN0 の概要

• エントリーDOI: 10.2210/pdb5vn0/pdb
• 関連するPDBエントリー: 5VOH
• 分子名称: NAD(FAD)-dependent dehydrogenase, FLAVIN-ADENINE DINUCLEOTIDE, OXYGEN MOLECULE, ... (6 entities in total)
• 機能のキーワード: substrate bound, redox active cysteine, water-forming oxidase, oxidoreductase
• 由来する生物種: Lactobacillus brevis (strain ATCC 367 / JCM 1170)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 461700.59

構造登録者

Cracan, V.,Grabarek, Z. (登録日: 2017-04-28, 公開日: 2017-08-02, 最終更新日: 2023-10-04)

主引用文献

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

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: 28805804
DOI: 10.1038/nchembio.2454

実験手法

X-RAY DIFFRACTION (2.001 Å)