1QUE

X-RAY STRUCTURE OF THE FERREDOXIN:NADP+ REDUCTASE FROM THE CYANOBACTERIUM ANABAENA PCC 7119 AT 1.8 ANGSTROMS

1QUE の概要

• エントリーDOI: 10.2210/pdb1que/pdb
• 分子名称: FERREDOXIN--NADP+ REDUCTASE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, flavoprotein, nadp, fad, thylakoid membrane, hycobilisome, fnr, nadp+ reductase
• 由来する生物種: Nostoc sp.
• 細胞内の位置: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side: P21890
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34923.29

構造登録者

Serre, L.,Frey, M.,Vellieux, F.M.D. (登録日: 1996-07-06, 公開日: 1997-05-15, 最終更新日: 2024-04-03)

主引用文献

Serre, L.,Vellieux, F.M.,Medina, M.,Gomez-Moreno, C.,Fontecilla-Camps, J.C.,Frey, M.
X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP+ binding at 2.25 A resolution.
J.Mol.Biol., 263:20-39, 1996

PubMed Abstract: The crystal structure of the ferredoxin:NADP+ reductase (FNR) from the cyanobacterium Anabaena PCC 7119 has been determined at 2.6 A resolution by multiple isomorphous replacement and refined using 15.0 A to 1.8 A data, collected at 4 degrees C, to an R-factor of 0.172. The model includes 303 residues, the flavin adenine dinucleotide cofactor (FAD), one sulfate ion located at the putative NADP+ binding site and 328 water molecule sites. The structure of Anabaena FNR, including FAD, a network of intrinsic water molecules and a large hydrophobic cavity in the C-terminal domain, resembles that of the spinach enzyme. The major differences concern the additional short alpha-helix (residues 172 to 177 in Anabaena FNR) and residues Arg 100 and Arg 233 which binds NADP+ instead of Lys 116 and Lys 244 in the spinach enzyme. Crystals of a complex of Anabaena FNR with NADP+ were obtained. The model of the complex has been refined using 15 A to 2.25 A X-ray data, collected at -170 degrees C, to an R-factor of 0.186. This model includes 295 residues, FAD, the full NADP+ (with an occupancy of 0.8) and 444 water molecules. The 2'-5' adenine moiety of NADP+ binds to the protein as 2'-phospho-5'-AMP to the spinach FNR. The nicotinamide moiety is turned towards the surface of the protein instead of stacking onto the FAD isoalloxazine ring as would be required for hydride transfer. The model of the complex agrees with previous biochemical studies as residues Arg 100 and Arg 233 are involved in NADP+ binding and residues Arg77, Lys 53 and Lys 294, located on the FAD side of the enzyme, remain free to interact with ferredoxin and flavodoxin, the physiological partners of ferredoxin: NADP reductase.

PubMed: 8890910
DOI: 10.1006/jmbi.1996.0553

実験手法

X-RAY DIFFRACTION (1.8 Å)