4B4D

Crystal structure of FAD-containing ferredoxin-NADP reductase from Xanthomonas axonopodis pv. citri

4B4D の概要

• エントリーDOI: 10.2210/pdb4b4d/pdb
• 分子名称: FERREDOXIN-NADP REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: XANTHOMONAS AXONOPODIS PV. CITRI STR. 306
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30608.81

構造登録者

Martinez-Julvez, M.,Orellano, E.G.,Tondo, M.L.,Hurtado-Guerrero, R.,Medina, M.,Ceccarelli, E.A.,Sanchez-Azqueta, A. (登録日: 2012-07-30, 公開日: 2013-08-21, 最終更新日: 2023-12-20)

主引用文献

Tondo, M.L.,Hurtado-Guerrero, R.,Sanchez-Azqueta, A.,Ceccarelli, E.A.,Medina, M.,Orellano, E.G.,Martinez-Julvez, M.
Crystal Structure of Fad-Containing Ferredoxin- Nadp Reductase from Xanthomonas Axonopodis Pv. Citri
Biomed Res Int, 2013:06572-, 2013

PubMed Abstract: We have solved the structure of ferredoxin-NADP(H) reductase, FPR, from the plant pathogen Xanthomonas axonopodis pv. citri, responsible for citrus canker, at a resolution of 1.5 Å. This structure reveals differences in the mobility of specific loops when compared to other FPRs, probably unrelated to the hydride transfer process, which contributes to explaining the structural and functional divergence between the subclass I FPRs. Interactions of the C-terminus of the enzyme with the phosphoadenosine of the cofactor FAD limit its mobility, thus affecting the entrance of nicotinamide into the active site. This structure opens the possibility of rationally designing drugs against the X. axonopodis pv. citri phytopathogen.

PubMed: 23984418
DOI: 10.1155/2013/906572

実験手法

X-RAY DIFFRACTION (1.5 Å)