3VO2
Crystal structure of Zea mays leaf ferredoxin-NADP+ reductase III
3VO2 の概要
| エントリーDOI | 10.2210/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 | |
| 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: 22805436DOI: 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) |
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