ArticleActa crystallographica. Section F, Structural biology communications2014
Structure determination of a sugar-binding protein from the phytopathogenic bacterium Xanthomonas citri.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 9 citations in OpenAlex.
- Insights into the recognition of cyclic α-(1→6)-glucan by a solute-binding protein of an ABC transporter from Tepidibacillus decaturensis.The Journal of biological chemistry · 2026Article
- Expression, purification, and characterization of diacylated Lipo-YcjN frombioRxiv : the preprint server for biology · 2024Article
- Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway.PloS one · 2020Article
- Structural and thermodynamic insights into β-1,2-glucooligosaccharide capture by a solute-binding protein inThe Journal of biological chemistry · 2018Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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