1OGI

FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY AND ALA 160 REPLACED BY THR (T155G-A160T)

1OGI の概要

• エントリーDOI: 10.2210/pdb1ogi/pdb
• 関連するPDBエントリー: 1B2R 1BJK 1BQE 1E62 1E63 1E64 1EWY 1GJR 1GO2 1GR1 1H42 1H85 1OGJ 1QGZ 1QH0 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, fad, fnr, nadp reductase
• 由来する生物種: ANABAENA SP. (STRAIN PCC 7119)
• 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: 34909.26

構造登録者

Hermoso, J.A.,Mayoral, T.,Julvez, M.M.,Medina, M.,Sanz-Aparicio, J.,Gomez-Moreno, C. (登録日: 2003-05-06, 公開日: 2003-09-25, 最終更新日: 2023-12-13)

主引用文献

Tejero, J.,Martinez-Julvez, M.,Mayoral, T.,Luquita, A.,Sanz-Aparicio, J.,Hermoso, J.A.,Hurley, J.K.,Tollin, G.,Gomez-Moreno, C.,Medina, M.
Involvement of the Pyrophosphate and the 2'-Phosphate Binding Regions of Ferredoxin-Nadp+ Reductase in Coenzyme Specificity.
J.Biol.Chem., 278:49203-, 2003

PubMed Abstract: Previous studies indicated that the determinants of coenzyme specificity in ferredoxin-NADP+ reductase (FNR) from Anabaena are situated in the 2'-phosphate (2'-P) NADP+ binding region, and also suggested that other regions must undergo structural rearrangements of the protein backbone during coenzyme binding. Among the residues involved in such specificity could be those located in regions where interaction with the pyrophosphate group of the coenzyme takes place, namely loops 155-160 and 261-268 in Anabaena FNR. In order to learn more about the coenzyme specificity determinants, and to better define the structural basis of coenzyme binding, mutations in the pyrophosphate and 2'-P binding regions of FNR have been introduced. Modification of the pyrophosphate binding region, involving residues Thr-155, Ala-160, and Leu-263, indicates that this region is involved in determining coenzyme specificity and that selected alterations of these positions produce FNR enzymes that are able to bind NAD+. Thus, our results suggest that slightly different structural rearrangements of the backbone chain in the pyrophosphate binding region might determine FNR specificity for the coenzyme. Combined mutations at the 2'-P binding region, involving residues Ser-223, Arg-224, Arg-233, and Tyr-235, in combination with the residues mentioned above in the pyrophosphate binding region have also been carried out in an attempt to increase the FNR affinity for NAD+/H. However, in most cases the analyzed mutants lost the ability for NADP+/H binding and electron transfer, and no major improvements were observed with regard to the efficiency of the reactions with NAD+/H. Therefore, our results confirm that determinants for coenzyme specificity in FNR are also situated in the pyrophosphate binding region and not only in the 2'-P binding region. Such observations also suggest that other regions of the protein, yet to be identified, might also be involved in this process.

PubMed: 14500716
DOI: 10.1074/JBC.M307934200

実験手法

X-RAY DIFFRACTION (1.64 Å)