8QG1

Crystal structure of oxidized respiratory Complex I subunits NuoEF from Aquifex aeolicus bound to ADP-ribose

8QG1 の概要

• エントリーDOI: 10.2210/pdb8qg1/pdb
• 分子名称: NADH-quinone oxidoreductase subunit E, SODIUM ION, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, ... (12 entities in total)
• 機能のキーワード: complex i, respiratory chain, inhibitor, nadh-binding, oxidoreductase
• 由来する生物種: Aquifex aeolicus VF5; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 138536.64

構造登録者

Wohlwend, D.,Friedrich, T. (登録日: 2023-09-05, 公開日: 2024-04-03, 最終更新日: 2024-06-19)

主引用文献

Wohlwend, D.,Merono, L.,Bucka, S.,Ritter, K.,Jessen, H.J.,Friedrich, T.
Structures of 3-acetylpyridine adenine dinucleotide and ADP-ribose bound to the electron input module of respiratory complex I.
Structure, 32:715-, 2024

PubMed Abstract: Energy-converting NADH:ubiquinone oxidoreductase, respiratory complex I, is a major enzyme of energy metabolism that couples NADH oxidation and ubiquinone reduction with proton translocation. The NADH oxidation site features different enzymatic activities with various nucleotides. While the kinetics of these reactions are well described, only binding of NAD and NADH have been structurally characterized. Here, we report the structures of the electron input module of Aquifex aeolicus complex I with bound ADP-ribose and 3-acetylpyridine adenine dinucleotides at resolutions better than 2.0 Å. ADP-ribose acts as inhibitor by blocking the "ADP-handle" motif essential for nucleotide binding. The pyridine group of APADH is minimally offset from flavin, which could contribute to its poorer suitability as substrate. A comparison with other nucleotide co-structures surprisingly shows that the adenine ribose and the pyrophosphate moiety contribute most to nucleotide binding, thus all adenine dinucleotides share core binding modes to the unique Rossmann-fold in complex I.

PubMed: 38503292
DOI: 10.1016/j.str.2024.02.013

実験手法

X-RAY DIFFRACTION (2 Å)