1H85

FERREDOXIN:NADP+ REDUCTASE MUTANT WITH VAL 136 REPLACED BY LEU (V136L)

1H85 の概要

• エントリーDOI: 10.2210/pdb1h85/pdb
• 関連するPDBエントリー: 1B2R 1BJK 1E62 1E63 1E64 1QUE 1QUF
• 分子名称: FERREDOXIN--NADP REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, flavoprotein, nadp, electron transport
• 由来する生物種: NOSTOC SP.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34098.35

構造登録者

Hermoso, J.A.,Mayoral, T.,Medina, M.,Sanz-Aparicio, J.,Gomez-Moreno, C. (登録日: 2001-01-24, 公開日: 2001-11-28, 最終更新日: 2023-12-13)

主引用文献

Marti-Nez-Julvez, M.,Nogues, I.,Faro, M.,Hurley, J.K.,Brodie, T.B.,Mayoral, T.,Sanz-Aparicio, J.,Hermoso, J.A.,Stankovich, M.T.,Medina, M.,Tollin, G.,Gomez-Moreno, C.
Role of a Cluster of Hydrophobic Residues Near the Fad Cofactor in Anabaena Pcc 7119 Ferredoxin-Nadp+ Reductase for Optimal Complex Formation and Electron Transfer to Ferredoxin
J.Biol.Chem., 276:27498-, 2001

PubMed Abstract: In the ferredoxin-NADP(+) reductase (FNR)/ferredoxin (Fd) system, an aromatic amino acid residue on the surface of Anabaena Fd, Phe-65, has been shown to be essential for the electron transfer (ET) reaction. We have investigated further the role of hydrophobic interactions in complex stabilization and ET between these proteins by replacing three hydrophobic residues, Leu-76, Leu-78, and Val-136, situated on the FNR surface in the vicinity of its FAD cofactor. Whereas neither the ability of FNR to accept electrons from NADPH nor its structure appears to be affected by the introduced mutations, different behaviors with Fd are observed. Thus, the ET interaction with Fd is almost completely lost upon introduction of negatively charged side chains. In contrast, only subtle changes are observed upon conservative replacement. Introduction of Ser residues produces relatively sizable alterations of the FAD redox potential, which can explain the modified behavior of these mutants. The introduction of bulky aromatic side chains appears to produce rearrangements of the side chains at the FNR/Fd interaction surface. Thus, subtle changes in the hydrophobic patch influence the rates of ET to and from Fd by altering the binding constants and the FAD redox potentials, indicating that these residues are especially important in the binding and orientation of Fd for efficient ET. These results are consistent with the structure reported for the Anabaena FNR.Fd complex.

PubMed: 11342548
DOI: 10.1074/JBC.M102112200

実験手法

X-RAY DIFFRACTION (2.3 Å)