1FND

REFINED CRYSTAL STRUCTURE OF SPINACH FERREDOXIN REDUCTASE AT 1.7 ANGSTROMS RESOLUTION: OXIDIZED, REDUCED, AND 2'-PHOSPHO-5'-AMP BOUND STATES

「2FNR」から置き換えられました

1FND の概要

• エントリーDOI: 10.2210/pdb1fnd/pdb
• 分子名称: FERREDOXIN-NADP+ REDUCTASE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase (nadp+(a), ferredoxin(a))
• 由来する生物種: Spinacia oleracea (spinach)
• 細胞内の位置: Plastid, chloroplast stroma: P00455
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36690.51

構造登録者

Bruns, C.M.,Karplus, P.A. (登録日: 1995-01-05, 公開日: 1995-04-20, 最終更新日: 2024-02-07)

主引用文献

Bruns, C.M.,Karplus, P.A.
Refined crystal structure of spinach ferredoxin reductase at 1.7 A resolution: oxidized, reduced and 2'-phospho-5'-AMP bound states.
J.Mol.Biol., 247:125-145, 1995

PubMed Abstract: The crystal structure of spinach ferredoxin-NADP(+)-oxidoreductase (FNR), determined by multiple isomorphous replacement at 2.6 A resolution, has been refined at 1.7 A resolution to an R-factor of 17.9%. The structure of FNR bound to the competitive inhibitor 2'-phospho-5'-AMP (P-AMP) has also been refined at 1.7 A to an R-factor of 17.4% and dithionite-reduced/P-AMP-bound FNR has been refined at 2.0 A to an R-factor of 14.9%. The P-AMP-bound structure was used to construct a model for the binding of NADP+. Over 200 solvation sites were included in each structure, and many of the best defined solvation sites stabilize buried turns. A bulk solvent correction obviated the need for a low-resolution data cutoff. An acidic side-chain likely to be responsible for the low pH requirement for crystallization has been identified. Three large networks of the hydrophobic side-chains help define the FNR structure. One of these contains a large cavity far from the active site, which coincides with the lone site of sequence heterogeneity in FNR, and may provide a site for membrane attachment. The reduced structure shows that Ser96 moves toward atom N-5 of FAD and a water molecule moves toward atom N-1 of FAD, while the flavin moiety remains planar. Possible sources of a proton that must be picked up upon reduction are discussed.

PubMed: 7897656
DOI: 10.1006/jmbi.1994.0127

実験手法

X-RAY DIFFRACTION (1.7 Å)