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Structure determination of a sugar-binding protein from the phytopathogenic bacterium Xanthomonas citri

AuthorsMedrano, Francisco Javier; Santos de Souza, Cristiane; Romero, Antonio ; Balan, Andrea
Issue Date5-May-2014
PublisherInternational Union of Crystallography
CitationActa Crystallographica Section F (2014) 70 (5) 564-571
AbstractThe uptake of maltose and related sugars in Gram-negative bacteria is mediated by an ABC transporter encompassing a periplasmic component (the maltosebinding protein or MalE), a pore-forming membrane protein (MalF and MalG) and a membrane-associated ATPase (MalK). In the present study, the structure determination of the apo form of the putative maltose/trehalose-binding protein (Xac-MalE) from the citrus pathogen Xanthomonas citri in space group P6522 is described. The crystals contained two protein molecules in the asymmetric unit and diffracted to 2.8 A ° resolution. Xac-MalE conserves the structural and functional features of sugar-binding proteins and a ligand-binding pocket with similar characteristics to eight different orthologues, including the residues for maltose and trehalose interaction. This is the first structure of a sugar-binding protein from a phytopathogenic bacterium, which is highly conserved in all species from the Xanthomonas genus.
Description8 pág.-5 fig.-1 tab.
Publisher version (URL)http://dx.doi.org/10.1107/S2053230X14006578
Appears in Collections:(CIB) Artículos
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