Artículo
Crystal Structure of the FAD-Containing Ferredoxin-NADP+ Reductase from the Plant Pathogen Xanthomonas axonopodis pv. Citri
Tondo, Maria Laura
; Hurtado Guerrero, Ramon; Ceccarelli, Eduardo Augusto
; Medina, Milagros; Orellano, Elena Graciela
; Martínez Júlvez, Marta
Fecha de publicación:
07/2013
Editorial:
Hindawi Publishing Corporation
Revista:
BioMed Research International
ISSN:
2314-6141
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
We have solved the structure of ferredoxin-NADP(H) reductase, FPR, from the plant pathogenXanthomonas axonopodispv. citri, responsible for citrus canker, at a resolution of 1.5˚ A. 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 theX. axonopodispv. citri phytopathogen.
Palabras clave:
Reductasa
,
Flavoenzimas
,
Xanthomonas Axonopodis
,
Cristalografía
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Colecciones
Articulos(IBR)
Articulos de INST.DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Articulos de INST.DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Citación
Tondo, Maria Laura; Hurtado Guerrero, Ramon; Ceccarelli, Eduardo Augusto; Medina, Milagros; Orellano, Elena Graciela; et al.; Crystal Structure of the FAD-Containing Ferredoxin-NADP+ Reductase from the Plant Pathogen Xanthomonas axonopodis pv. Citri; Hindawi Publishing Corporation; BioMed Research International; 2013; 7-2013; 906572-906572
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