Crystal structure of the FAD-containing ferredoxin-NADP+ reductase from the plant pathogen Xanthomonas axonopodis pv. citri

Tondo, M.L. ; Hurtado-Guerrero, R. ; Ceccarelli, E.A. ; Medina, M. (Universidad de Zaragoza) ; Orellano, E.G. ; Martínez-Júlvez, M. (Universidad de Zaragoza)

Resumen: 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.

Idioma: Inglés

DOI: 10.1155/2013/906572

Año: 2013

Publicado en: BioMed Research International 2013, 906572 (2013), [6 pp.]
ISSN: 2314-6133

Factor impacto JCR: 0.0 (2013)

Categ. JCR: MEDICINE, RESEARCH & EXPERIMENTAL
Categ. JCR: BIOTECHNOLOGY & APPLIED MICROBIOLOGY

Financiación: info:eu-repo/grantAgreement/ES/DGA/B18
Financiación: info:eu-repo/grantAgreement/ES/MICINN/BIO2010-14983

Tipo y forma: Article (Published version)

Área (Departamento): Bioquímica y Biología Molecular (Departamento de Bioquímica y Biología Molecular y Celular)