Structural model and ligand interactions of the Xanthomonas axonopodis pv. citri oligopeptide-binding protein
Genet. mol. res. (Online)
;
6(4): 1169-1177, 2007. ilus, graf
Article
in English
| LILACS
| ID: lil-520032
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.
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Oligopeptides
/
Bacterial Proteins
/
Xanthomonas
/
Carrier Proteins
/
Lipoproteins
Language:
English
Journal:
Genet. mol. res. (Online)
Journal subject:
Molecular Biology
/
Genetics
Year:
2007
Type:
Article
Affiliation country:
Brazil
Institution/Affiliation country:
Universidade de São Paulo/BR
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