1QGA

PEA FNR Y308W MUTANT IN COMPLEX WITH NADP+

1QGA の概要

• エントリーDOI: 10.2210/pdb1qga/pdb
• 関連するPDBエントリー: 1QFY 1QFZ 1QG0
• 分子名称: PROTEIN (FERREDOXIN:NADP+ REDUCTASE), SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: flavoenzyme, photosynthesis, electron transfer, hydride transfer, oxidoreductase
• 由来する生物種: Pisum sativum (pea)
• 細胞内の位置: Plastid, chloroplast stroma: P10933
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72888.18

構造登録者

Deng, Z.,Aliverti, A.,Zanetti, G.,Arakaki, A.K.,Ottado, J.,Orellano, E.G.,Calcaterra, N.B.,Ceccarelli, E.A.,Carrillo, N.,Karplus, P.A. (登録日: 1999-04-18, 公開日: 1999-04-27, 最終更新日: 2024-12-25)

主引用文献

Deng, Z.,Aliverti, A.,Zanetti, G.,Arakaki, A.K.,Ottado, J.,Orellano, E.G.,Calcaterra, N.B.,Ceccarelli, E.A.,Carrillo, N.,Karplus, P.A.
A productive NADP+ binding mode of ferredoxin-NADP+ reductase revealed by protein engineering and crystallographic studies.
Nat.Struct.Biol., 6:847-853, 1999

PubMed Abstract: The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, none of these studies has yielded a productive geometry of the flavin-nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain. We used mutants of this residue (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at an angle of approximately 30 degrees, with the C4 atom 3 A from the flavin N5 atom.

PubMed: 10467097
DOI: 10.1038/12307

実験手法

X-RAY DIFFRACTION (2 Å)