Structure of an ABC transporter solute-binding protein specific for the amino sugars glucosamine and galactosamine.

  title={Structure of an ABC transporter solute-binding protein specific for the amino sugars glucosamine and galactosamine.},
  author={U. Yadava and M. Vetting and Nawar Al Obaidi and Michael S. Carter and J. Gerlt and S. Almo},
  journal={Acta crystallographica. Section F, Structural biology communications},
  volume={72 Pt 6},
  • U. Yadava, M. Vetting, +3 authors S. Almo
  • Published 2016
  • Chemistry, Medicine
  • Acta crystallographica. Section F, Structural biology communications
The 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… Expand
3 Citations
Periplasmic solute-binding proteins: Structure classification and chitooligosaccharide recognition.
The overall structural feature of the Vibrios CBPs is most similar to the cellobiose-binding orthologue from the hyperthermophilic bacterium Thermotoga maritima, which provides an opportunity to engineer the substrate specificity of the proteins and to control the uptake of chitinous and cellulosic nutrients in marine bacteria. Expand
The Fish Pathogen Aliivibrio salmonicida LFI1238 Can Degrade and Metabolize Chitin despite Gene Disruption in the Chitinolytic Pathway
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This study applies the use of solute-binding proteins for transport systems to the ATP-binding cassette transporters and reports the discovery of novel catabolic pathways for d-altritol and galactitol in Agrobacterium tumefaciens C58. Expand
Characterization of transport proteins for aromatic compounds derived from lignin: benzoate derivative binding proteins.
Characterization of this new class of transporters improves genomic annotation projects and provides insight into the metabolic potential of soil bacteria. Expand
Functional assignment of solute-binding proteins of ABC transporters using a fluorescence-based thermal shift assay.
The ability of the FTS assay to unambiguously identify preferential binding for several homologues of amino acid-binding proteins with known specificity and to functionally annotate proteins of unknown binding specificity is demonstrated. Expand
GxySBA ABC Transporter of Agrobacterium tumefaciens and Its Role in Sugar Utilization and vir Gene Expression
A putative ABC transporter encoded by the gxySBA operon is identified and shown to be involved in the utilization of glucose, xylose, fucose, and arabinose, which are also substrates for the ChvE-MmsAB ABC transporter, and the first characterized glucosamine ABC transporter is shown. Expand
Domain dislocation: a change of core structure in periplasmic binding proteins in their evolutionary history.
The present analysis shows that the unidirectional change of protein evolution is clearly deduced at the level of protein three-dimensional structure rather than thelevel of amino acid sequence, indicating that the change in the core structure occurred only once in the evolution of PBPs. Expand
The Use of Amino Sugars by Bacillus subtilis: Presence of a Unique Operon for the Catabolism of Glucosamine
The method to make multiple deletion mutations in B. subtilis employing an excisable spectinomycin resistance cassette and the contribution of the different genes of the nag and gam operons for their role in utilization of glucosamine and N-acetylglucosamine is analysed. Expand
Structure and mechanism of ATP-binding cassette transporters
  • K. Locher
  • Biology, Medicine
  • Philosophical Transactions of the Royal Society B: Biological Sciences
  • 2008
ATP-binding cassette (ABC) transporters constitute a large superfamily of integral membrane proteins that includes both importers and exporters. In recent years, several structures of complete ABCExpand
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Genetic studies show that Escherichia coli has three enzymes capable of phosphorylating glucose: soluble adenosine 5'-triphosphate-dependent glucokinase, which plays only a minor role in glucose metabolism; an enzyme II with high specificity for the D-glucose configuration; and another enzyme II, called mannosephosphotransferase, with broader specificity. Expand
Structural insights into ABC transporter mechanism.
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