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3MHP

FNR-recruitment to the thylakoid

3MHP の概要
エントリーDOI10.2210/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
Groll, M.,Alte, F.,Soll, J.,Boelter, B. (登録日: 2010-04-08, 公開日: 2010-10-27, 最終更新日: 2023-09-06)
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: 20974920
DOI: 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)
構造検証レポート
Validation report summary of 3mhp
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2026-02-11に公開中

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