4BPR

FERREDOXIN-NADP REDUCTASE MUTANT WITH TYR 79 REPLACED BY PHE (Y79F)

4BPR の概要

• エントリーDOI: 10.2210/pdb4bpr/pdb
• 分子名称: FERREDOXIN-NADP REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, flavoprotein
• 由来する生物種: ANABAENA 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: 34999.38

構造登録者

Herguedas, B.,Martinez-Julvez, M.,Sanchez-Azqueta, A.,Hervas, M.,Navarro, J.A.,Medina, M. (登録日: 2013-05-28, 公開日: 2013-11-20, 最終更新日: 2023-12-20)

主引用文献

Sanchez-Azqueta, A.,Herguedas, B.,Hurtado-Guerrero, R.,Hervas, M.,Navarro, J.A.,Martinez-Julvez, M.,Medina, M.
A Hydrogen Bond Network in the Active Site of Anabaena Ferredoxin-Nadp(+) Reductase Modulates its Catalytic Efficiency.
Biochim.Biophys.Acta, 1837:251-, 2013

PubMed Abstract: Ferredoxin-nicotinamide-adenine dinucleotide phosphate (NADP(+)) reductase (FNR) catalyses the production of reduced nicotinamide-adenine dinucleotide phosphate (NADPH) in photosynthetic organisms, where its flavin adenine dinucleotide (FAD) cofactor takes two electrons from two reduced ferredoxin (Fd) molecules in two sequential steps, and transfers them to NADP(+) in a single hydride transfer (HT) step. Despite the good knowledge of this catalytic machinery, additional roles can still be envisaged for already reported key residues, and new features are added to residues not previously identified as having a particular role in the mechanism. Here, we analyse for the first time the role of Ser59 in Anabaena FNR, a residue suggested by recent theoretical simulations as putatively involved in competent binding of the coenzyme in the active site by cooperating with Ser80. We show that Ser59 indirectly modulates the geometry of the active site, the interaction with substrates and the electronic properties of the isoalloxazine ring, and in consequence the electron transfer (ET) and HT processes. Additionally, we revise the role of Tyr79 and Ser80, previously investigated in homologous enzymes from plants. Our results probe that the active site of FNR is tuned by a H-bond network that involves the side-chains of these residues and that results to critical optimal substrate binding, exchange of electrons and, particularly, competent disposition of the C4n (hydride acceptor/donor) of the nicotinamide moiety of the coenzyme during the reversible HT event.

PubMed: 24200908
DOI: 10.1016/J.BBABIO.2013.10.010

実験手法

X-RAY DIFFRACTION (2 Å)