1DJL

THE CRYSTAL STRUCTURE OF HUMAN TRANSHYDROGENASE DOMAIN III WITH BOUND NADP

1DJL の概要

• エントリーDOI: 10.2210/pdb1djl/pdb
• 分子名称: TRANSHYDROGENASE DIII, SULFATE ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: rossmann fold dinucleotide binding fold reverse binding of nadp, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side (Potential): Q13423
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46426.43

構造登録者

White, S.A.,Peak, S.J.,Cotton, N.P.,Jackson, J.B. (登録日: 1999-12-03, 公開日: 2000-12-06, 最終更新日: 2024-02-07)

主引用文献

White, S.A.,Peake, S.J.,McSweeney, S.,Leonard, G.,Cotton, N.P.,Jackson, J.B.
The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria.
Structure Fold.Des., 8:1-12, 2000

PubMed Abstract: Transhydrogenase, located in the inner membranes of animal mitochondria and the cytoplasmic membranes of bacteria, couples the transfer of reducing equivalents between NAD(H) and NADP(H) to proton pumping. The protein comprises three subunits termed dI, dII and dIII. The dII component spans the membrane. The dI component, which contains the binding site for NAD(+)/NADH, and the dIII component, which has the binding site for NADP(+)/NADPH, protrude from the membrane. Proton pumping is probably coupled to changes in the binding affinities of dIII for NADP(+) and NADPH.

PubMed: 10673423
DOI: 10.1016/S0969-2126(00)00075-7

実験手法

X-RAY DIFFRACTION (2 Å)