6A7K

X-ray structure of NdhS from T. elongatus

6A7K の概要

• エントリーDOI: 10.2210/pdb6a7k/pdb
• 分子名称: Tlr0636 protein, ACETIC ACID (3 entities in total)
• 機能のキーワード: nadh dehydrogenase-like complex, ndh-1, cyclic electron flow (cef), ferredoxin, electron transport
• 由来する生物種: Thermosynechococcus elongatus (strain BP-1)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16567.22

構造登録者

Umeno, K.,Misumi, Y.,Tanaka, H.,Kurisu, G. (登録日: 2018-07-03, 公開日: 2019-01-16, 最終更新日: 2023-11-22)

主引用文献

Schuller, J.M.,Birrell, J.A.,Tanaka, H.,Konuma, T.,Wulfhorst, H.,Cox, N.,Schuller, S.K.,Thiemann, J.,Lubitz, W.,Setif, P.,Ikegami, T.,Engel, B.D.,Kurisu, G.,Nowaczyk, M.M.
Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer.
Science, 363:257-260, 2019

PubMed Abstract: Photosynthetic complex I enables cyclic electron flow around photosystem I, a regulatory mechanism for photosynthetic energy conversion. We report a 3.3-angstrom-resolution cryo-electron microscopy structure of photosynthetic complex I from the cyanobacterium The model reveals structural adaptations that facilitate binding and electron transfer from the photosynthetic electron carrier ferredoxin. By mimicking cyclic electron flow with isolated components in vitro, we demonstrate that ferredoxin directly mediates electron transfer between photosystem I and complex I, instead of using intermediates such as NADPH (the reduced form of nicotinamide adenine dinucleotide phosphate). A large rate constant for association of ferredoxin to complex I indicates efficient recognition, with the protein subunit NdhS being the key component in this process.

PubMed: 30573545
DOI: 10.1126/science.aau3613

実験手法

X-RAY DIFFRACTION (1.9 Å)