1B2R

FERREDOXIN-NADP+ REDUCTASE (MUTATION: E 301 A)

1B2R の概要

• エントリーDOI: 10.2210/pdb1b2r/pdb
• 分子名称: PROTEIN (FERREDOXIN-NADP+ REDUCTASE), SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, flavoprotein, nadp, fad, 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: 34996.45

構造登録者

Hermoso, J.A.,Mayoral, T.,Medina, M.,Martinez-Ripoll, M.,Martinez-Julvez, M.,Sanz-Aparicio, J.,Gomez-Moreno, C. (登録日: 1998-11-27, 公開日: 1999-12-15, 最終更新日: 2023-08-09)

主引用文献

Mayoral, T.,Medina, M.,Sanz-Aparicio, J.,Gomez-Moreno, C.,Hermoso, J.A.
Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by x-ray crystallography.
Proteins, 38:60-69, 2000

PubMed Abstract: The three-dimensional crystal structure of the Glu301Ala site-directed mutant of ferredoxin-NADP+ reductase from Anabaena PCC 7119 has been determined at 1.8A resolution by x-ray diffraction. The overall folding of the Glu301Ala FNR mutant shows no significant differences with respect to that of the wild-type enzyme. However, interesting conformational changes are detected in the side chain of another glutamate residue, Glu139, which now points towards the FAD cofactor in the active center cavity. The new conformation of the Glu139 side chain is stabilized by a network of five hydrogen bonds to several water molecules, which seem to hold the carboxylate side chain in a rather fixed position. This interacting network connects the Glu139 side chain to the Ser80 side chain through a series of three water molecules. These observations are discussed in terms of the reactivity of Glu301Ala ferredoxin-NADP+ reductase towards its substrates, and the role of Glu301 in the catalysis is re-examined. Moreover, a structural explanation of the different reoxidation properties of this mutant is given on the basis of the reported structure by modeling the hypothetical flavin C(4a)-hydroperoxide intermediate. The model shows that the distal oxygen of the peroxide anion could be in an appropriate situation to act as the proton donor in the reoxidation process.

PubMed: 10651039
DOI: 10.1002/(SICI)1097-0134(20000101)38:1<60::AID-PROT7>3.3.CO;2-2

実験手法

X-RAY DIFFRACTION (1.8 Å)