9EVX

cryoEM structure of Photosystem II averaged across S2-S3 states at 1.71 Angstrom resolution

これはPDB形式変換不可エントリーです。

9EVX の概要

• エントリーDOI: 10.2210/pdb9evx/pdb
• EMDBエントリー: 50019
• 分子名称: Photosystem II protein D1 1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (36 entities in total)
• 機能のキーワード: photosystem ii core complex, mn cluster, water oxidation, metal binding protein
• 由来する生物種: Thermosynechococcus vestitus BP-1; 詳細
• タンパク質・核酸の鎖数: 38
• 化学式量合計: 759946.36

構造登録者

Hussein, R.,Graca, A.,Zouni, A.,Messinger, J.,Schroder, W.P. (登録日: 2024-04-02, 公開日: 2024-06-12, 最終更新日: 2024-11-06)

主引用文献

Hussein, R.,Graca, A.,Forsman, J.,Aydin, A.O.,Hall, M.,Gaetcke, J.,Chernev, P.,Wendler, P.,Dobbek, H.,Messinger, J.,Zouni, A.,Schroder, W.P.
Cryo-electron microscopy reveals hydrogen positions and water networks in photosystem II.
Science, 384:1349-1355, 2024

PubMed Abstract: Photosystem II starts the photosynthetic electron transport chain that converts solar energy into chemical energy and thus sustains life on Earth. It catalyzes two chemical reactions: water oxidation to molecular oxygen and plastoquinone reduction. Coupling of electron and proton transfer is crucial for efficiency; however, the molecular basis of these processes remains speculative owing to uncertain water binding sites and the lack of experimentally determined hydrogen positions. We thus collected high-resolution cryo-electron microscopy data of fully hydrated photosystem II from the thermophilic cyanobacterium to a final resolution of 1.71 angstroms. The structure reveals several previously undetected partially occupied water binding sites and more than half of the hydrogen and proton positions. This clarifies the pathways of substrate water binding and plastoquinone B protonation.

PubMed: 38900892
DOI: 10.1126/science.adn6541

実験手法

ELECTRON MICROSCOPY (1.71 Å)