3MHP
FNR-recruitment to the thylakoid
3MHP の概要
| エントリーDOI | 10.2210/pdb3mhp/pdb |
| 関連するPDBエントリー | 1QFY 1QFZ 1QG0 1QGA |
| 分子名称 | Ferredoxin--NADP reductase, leaf isozyme, chloroplastic, TIC62_peptide, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
| 機能のキーワード | fnr, oxidoreductase, thylakoid membrane, proton-flux, poly proline ii helix, self assembly, nadp(h) |
| 由来する生物種 | Pisum sativum (garden pea,peas) 詳細 |
| 細胞内の位置 | Plastid, chloroplast stroma: P10933 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 71548.46 |
| 構造登録者 | |
| 主引用文献 | Alte, F.,Stengel, A.,Benz, J.P.,Petersen, E.,Soll, J.,Groll, M.,Bolter, B. Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner. Proc.Natl.Acad.Sci.USA, 107:19260-19265, 2010 Cited by PubMed Abstract: Ferredoxin:NADPH oxidoreductase (FNR) is a key enzyme of photosynthetic electron transport required for generation of reduction equivalents. Recently, two proteins were found to be involved in membrane-anchoring of FNR by specific interaction via a conserved Ser/Pro-rich motif: Tic62 and Trol. Our crystallographic study reveals that the FNR-binding motif, which forms a polyproline type II helix, induces self-assembly of two FNR monomers into a back-to-back dimer. Because binding occurs opposite to the FNR active sites, its activity is not affected by the interaction. Surface plasmon resonance analyses disclose a high affinity of FNR to the binding motif, which is strongly increased under acidic conditions. The pH of the chloroplast stroma changes dependent on the light conditions from neutral to slightly acidic in complete darkness or to alkaline at saturating light conditions. Recruiting of FNR to the thylakoids could therefore represent a regulatory mechanism to adapt FNR availability/activity to photosynthetic electron flow. PubMed: 20974920DOI: 10.1073/pnas.1009124107 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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