A. Moutran, A. Balan, L.C.S. Ferreira, A. Giorgetti, A. Tramontano, R.C.C. Ferreira
Published December 20, 2007
Genet. Mol. Res. 6 (4): 1169-1177 (2007)

About the authors
A. Moutran, A. Balan, L.C.S. Ferreira, A. Giorgetti, A. Tramontano, R.C.C. Ferreira

Corresponding author
R.C.C. Ferreira
E-mail: ritacafe@usp.br

ABSTRACT

The oligopeptide-binding protein, OppA, ushers oligopeptide substrates to the membrane-associated oligopeptide permease (Opp), a multi-component ABC-type transporter involved in the uptake of oligopeptides by several bacterial species. In the present study, we report a structural model and an oligopeptide docking analysis of the OppA protein expressed by Xanthomonas axonopodis pv. citri (X. citri), the etiological agent of citrus canker. The X. citri OppA structural model showed a conserved three-dimensional structure, irrespective of the low amino acid identities with previously defined structures of Bacillus subtilis and Salmonella typhimurium orthologs. Oligopeptide docking analysis carried out with the proposed model indicated that the X. citri OppA preferentially binds tri- and tetrapeptides. The present study represents the first structural analysis of an OppA ortholog expressed by a phytopathogen and contributes to the understanding of the physiology and nutritional strategies of X. citri.

Key words: Oligopeptide-binding protein, Opp, ABC transport, Xanthomonas, Structural model