Structural highlights
FunctionPublication Abstract from PubMedThe uptake of exogenous solutes by prokaryotes is mediated by transport systems embedded in the plasma membrane. In many cases, a solute-binding protein (SBP) is utilized to bind ligands with high affinity and deliver them to the membrane-bound components responsible for translocation into the cytoplasm. In the present study, Avi_5305, an Agrobacterium vitis SBP belonging to Pfam13407, was screened by differential scanning fluorimetry (DSF) and found to be stabilized by D-glucosamine and D-galactosamine. Avi_5305 is the first protein from Pfam13407 shown to be specific for amino sugars, and co-crystallization resulted in structures of Avi_5305 bound to D-glucosamine and D-galactosamine. Typical of Pfam13407, Avi_5305 consists of two alpha/beta domains linked through a hinge region, with the ligand-binding site located in a cleft between the two domains. Comparisons with Escherichia coli ribose-binding protein suggest that a cation-pi interaction with Tyr168 provides the specificity for D-glucosamine/D-galactosamine over D-glucose/D-galactose. Structure of an ABC transporter solute-binding protein specific for the amino sugars glucosamine and galactosamine.,Yadava U, Vetting MW, Al Obaidi N, Carter MS, Gerlt JA, Almo SC Acta Crystallogr F Struct Biol Commun. 2016 Jun 1;72(Pt 6):467-72. doi:, 10.1107/S2053230X16007500. Epub 2016 May 23. PMID:27303900[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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