Molecular and structural analysis of maltose binding protein (MalE) of Xanthomonas axonopodis pv citri. / Análise molecular e estrutural da proteína ligadora de maltose (MalE) de Xanthomonas axonopodis pv. citri.

AUTOR(ES)
DATA DE PUBLICAÇÃO

2009

RESUMO

Maltose uptake in bacteria is mediated by an ABC transporter comprising a substrate binding protein (MalE), two transmembrane proteins, and one ATPase. In the present study, we describe the cloning, expression and biochemical as well as structural analyses of the MalE protein of the phytopagen Xanthomonas axonopodis pv citri (Xac). The malE gene of Xac was cloned in the pET28a expression vector, the recombinant protein was expressed in Escherichia coli and, subsequently, purified by nickel affinity chromatography. Samples of soluble protein were analyzed regarding secondary structure, interaction with putative ligants and stability under different physico-chemical conditions. Crystallization trials were carried out under different conditions, one particular condition yielded crystal with a P6122space group, but the structure was not solved. Based on known ortholog structures, a structural model for Xac MalE was obtained allowing interaction with modeled threhalose and maltose. Structural models the transmembrane (LacF and LacG) and ATPase (UgpC) components were also obtained. The present results represent an important contribution to the knowledge of the physiology and transporter systems found in Xac.

ASSUNTO(S)

spectroscopy xanthomonas axonopodis pv citri cristalografia microbiology transportadores do tipo abc crystallography modelagem molecular molecular modelling microbiologia maltose xanthomonas axonopodis pv citri espectroscopia maltose abc transporters

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