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3VO2

Crystal structure of Zea mays leaf ferredoxin-NADP+ reductase III

3VO2 の概要
エントリーDOI10.2210/pdb3vo2/pdb
関連するPDBエントリー1GAW 3VO1
分子名称Putative uncharacterized protein, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
機能のキーワードrossmann fold, oxidoreductase, fad binding
由来する生物種Zea mays (maize)
タンパク質・核酸の鎖数2
化学式量合計71318.95
構造登録者
Muraki, N.,Hase, T.,Kurisu, G. (登録日: 2012-01-18, 公開日: 2012-12-05, 最終更新日: 2023-11-08)
主引用文献Twachtmann, M.,Altmann, B.,Muraki, N.,Voss, I.,Okutani, S.,Kurisu, G.,Hase, T.,Hanke, G.T.
N-terminal structure of maize ferredoxin:NADP+ reductase determines recruitment into different thylakoid membrane complexes
Plant Cell, 24:2979-2991, 2012
Cited by
PubMed Abstract: To adapt to different light intensities, photosynthetic organisms manipulate the flow of electrons through several alternative pathways at the thylakoid membrane. The enzyme ferredoxin:NADP(+) reductase (FNR) has the potential to regulate this electron partitioning because it is integral to most of these electron cascades and can associate with several different membrane complexes. However, the factors controlling relative localization of FNR to different membrane complexes have not yet been established. Maize (Zea mays) contains three chloroplast FNR proteins with totally different membrane association, and we found that these proteins have variable distribution between cells conducting predominantly cyclic electron transport (bundle sheath) and linear electron transport (mesophyll). Here, the crystal structures of all three enzymes were solved, revealing major structural differences at the N-terminal domain and dimer interface. Expression in Arabidopsis thaliana of maize FNRs as chimeras and truncated proteins showed the N-terminal determines recruitment of FNR to different membrane complexes. In addition, the different maize FNR proteins localized to different thylakoid membrane complexes on expression in Arabidopsis, and analysis of chlorophyll fluorescence and photosystem I absorbance demonstrates the impact of FNR location on photosynthetic electron flow.
PubMed: 22805436
DOI: 10.1105/tpc.111.094532
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.39 Å)
構造検証レポート
Validation report summary of 3vo2
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2026-02-04に公開中

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