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6KMX

Structure of PSI from H. hongdechloris grown under far-red light condition

これはPDB形式変換不可エントリーです。
6KMX の概要
エントリーDOI10.2210/pdb6kmx/pdb
関連するPDBエントリー6KMW
EMDBエントリー0727
分子名称Photosystem I P700 chlorophyll a apoprotein A1, CHLOROPHYLL A ISOMER, CHLOROPHYLL A, ... (21 entities in total)
機能のキーワードphotosystem i, electron transport
由来する生物種Halomicronema hongdechloris C2206
詳細
タンパク質・核酸の鎖数27
化学式量合計1011731.07
構造登録者
Kato, K.,Nagao, R.,Shen, J.R.,Miyazaki, N.,Akita, F. (登録日: 2019-08-01, 公開日: 2020-01-15, 最終更新日: 2024-03-27)
主引用文献Kato, K.,Shinoda, T.,Nagao, R.,Akimoto, S.,Suzuki, T.,Dohmae, N.,Chen, M.,Allakhverdiev, S.I.,Shen, J.R.,Akita, F.,Miyazaki, N.,Tomo, T.
Structural basis for the adaptation and function of chlorophyll f in photosystem I.
Nat Commun, 11:238-238, 2020
Cited by
PubMed Abstract: Chlorophylls (Chl) play pivotal roles in energy capture, transfer and charge separation in photosynthesis. Among Chls functioning in oxygenic photosynthesis, Chl f is the most red-shifted type first found in a cyanobacterium Halomicronema hongdechloris. The location and function of Chl f in photosystems are not clear. Here we analyzed the high-resolution structures of photosystem I (PSI) core from H. hongdechloris grown under white or far-red light by cryo-electron microscopy. The structure showed that, far-red PSI binds 83 Chl a and 7 Chl f, and Chl f are associated at the periphery of PSI but not in the electron transfer chain. The appearance of Chl f is well correlated with the expression of PSI genes induced under far-red light. These results indicate that Chl f functions to harvest the far-red light and enhance uphill energy transfer, and changes in the gene sequences are essential for the binding of Chl f.
PubMed: 31932639
DOI: 10.1038/s41467-019-13898-5
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.41 Å)
構造検証レポート
Validation report summary of 6kmx
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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