Structural model and ligand interactions of the Xanthomonas axonopodis pv. citri oligopeptide-binding protein.
نویسندگان
چکیده
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.
منابع مشابه
Production of the refolded oligopeptide-binding protein (OppA) encoded by the citrus pathogen Xanthomonas axonopodis pv. Citri.
The oligopeptide-binding protein, OppA, binds and ushers oligopeptide substrates to the membrane-associated oligopeptide permease (Opp), a multi-component ABC-type transporter involved in the uptake of oligopeptides expressed by several bacterial species. In the present study, we report the cloning, purification, refolding and conformational analysis of a recombinant OppA protein derived from X...
متن کاملشباهت الگوی الکتروفورز پروتئین استرینهای Xanthomonas axonopodis pv. citri جداشده از مرکبات استانهای هرمزگان وکرمان با استرینهای برخی دیگر از گونههای Xanthomonas
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متن کاملشباهت الگوی الکتروفورز پروتئین استرینهای Xanthomonas axonopodis pv. citri جداشده از مرکبات استانهای هرمزگان وکرمان با استرینهای برخی دیگر از گونههای Xanthomonas
Protein electrophoretic pattern similarity among 21 strains of Xanthomonas axonopodis pv. citri isolated from Hormozgan and Kerman provinces together with the representatives of reference strains of X.a. pv. citri and X. a. pv. aurantifoli and 246 strains of the other Xanthomonas spp. including : X. a. pv. citri, X. a. pv. glycins, X. a. pv. manihotis, X. c. pv. campestris, X. a. pv. phaseoli, ...
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Maltose-binding protein is the periplasmic component of the ABC transporter responsible for the uptake of maltose/maltodextrins. The Xanthomonas axonopodis pv. citri maltose-binding protein MalE has been crystallized at 293 K using the hanging-drop vapour-diffusion method. The crystal belonged to the primitive hexagonal space group P6(1)22, with unit-cell parameters a = 123.59, b = 123.59, c = ...
متن کاملCyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri.
The protein Clp from Xanthomonas axonopodis pv. citri regulates pathogenesis and is a member of the CRP (cyclic AMP receptor protein) superfamily. We show that unlike the DNA-binding activity of other members of this family, the DNA-binding activity of Clp is allosterically inhibited by its effector and that cyclic di-GMP serves as that effector at physiological concentrations.
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ورودعنوان ژورنال:
- Genetics and molecular research : GMR
دوره 6 4 شماره
صفحات -
تاریخ انتشار 2007