Structure determination of a sugar‐binding protein from the phytopathogenic bacterium Xanthomonas citri. Issue 5 (1st May 2014)

• Record Type: Journal Article
• Authors: Medrano, Francisco Javier; de Souza, Cristiane Santos; Romero, Antonio; Balan, Andrea
• Is Part Of: Acta crystallographica. Volume 70:Issue 5(2014:May)
• Page Start: 564
• Page End: 571
• Publication Date: 2014-05-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14006578
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Xanthomonas citri</italic> in space group <italic>P</italic>6₅22 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 <italic>Xanthomonas</italic> genus.</p> </abstract>