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3uor
From Proteopedia
Revision as of 06:54, 24 September 2014 by OCA (Talk | contribs)
3uor is a 2 chain structure with sequence from Xanac. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
The uptake of maltose and related sugars in Gram-negative bacteria is mediated by an ABC transporter encompassing a periplasmic component (the maltose-binding 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.
Structure determination of a sugar-binding protein from the phytopathogenic bacterium Xanthomonas citri.,Medrano FJ, de Souza CS, Romero A, Balan A Acta Crystallogr F Struct Biol Commun. 2014 May;70(Pt 5):564-71. doi:, 10.1107/S2053230X14006578. Epub 2014 Apr 17. PMID:24817711[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Medrano FJ, de Souza CS, Romero A, Balan A. Structure determination of a sugar-binding protein from the phytopathogenic bacterium Xanthomonas citri. Acta Crystallogr F Struct Biol Commun. 2014 May;70(Pt 5):564-71. doi:, 10.1107/S2053230X14006578. Epub 2014 Apr 17. PMID:24817711 doi:http://dx.doi.org/10.1107/S2053230X14006578
