3UOR

The structure of the sugar-binding protein MalE from the phytopathogen Xanthomonas citri

Summary for 3UOR

• Entry DOI: 10.2210/pdb3uor/pdb
• Descriptor: ABC transporter sugar binding protein (2 entities in total)
• Functional Keywords: alfa/beta protein, periplasmic-binding protein, maltose, sugar binding protein
• Biological source: Xanthomonas axonopodis pv. citri
• Total number of polymer chains: 2
• Total formula weight: 102771.69

Authors

Medrano, F.J.,Souza, C.S.,Balan, A. (deposition date: 2011-11-17, release date: 2011-12-14, Last modification date: 2024-02-28)

Primary citation

Medrano, F.J.,de Souza, C.S.,Romero, A.,Balan, A.
Structure determination of a sugar-binding protein from the phytopathogenic bacterium Xanthomonas citri.
Acta Crystallogr F Struct Biol Commun, 70:564-571, 2014

PubMed Abstract: 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 Å 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.

PubMed: 24817711
DOI: 10.1107/S2053230X14006578

Experimental method

X-RAY DIFFRACTION (2.202 Å)