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BioMed Research International
Volume 2013 (2013), Article ID 906572, 6 pages
http://dx.doi.org/10.1155/2013/906572
Research Article

Crystal Structure of the FAD-Containing Ferredoxin-NADP+ Reductase from the Plant Pathogen Xanthomonas axonopodis pv. citri

1Molecular Biology Division, Instituto de Biología Molecular y Celular de Rosario (IBR), CONICET, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, S2002LRK Rosario, Argentina
2Fundación ARAID, Edificio Pignatelli 36, 50004 Zaragoza, Spain
3Institute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit BIFI-Rocasolano, Universidad de Zaragoza, 50018 Zaragoza, Spain
4Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Pedro Cerbuna 12, Universidad de Zaragoza, 50009 Zaragoza, Spain

Received 2 May 2013; Accepted 7 July 2013

Academic Editor: Stefan Knapp

Copyright © 2013 María Laura Tondo et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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.