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

Umesh Yadava, Matthew W. Vetting, Nawar Al Obaidi, Michael S. Carter, John A. Gerlt, Steven C. Almo

Research output: Contribution to journalArticle

Abstract

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-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 α/β 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-π interaction with Tyr168 provides the specificity for d-glucosamine/d-galactosamine over d-glucose/d-galactose.

Original languageEnglish (US)
Pages (from-to)467-472
Number of pages6
JournalActa Crystallographica Section:F Structural Biology Communications
Volume72
DOIs
StatePublished - Jan 1 2016

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Keywords

  • Agrobacterium vitis
  • Avi-5305
  • Pfam13407
  • Thermofluor
  • differential scanning fluorimetry
  • solute-binding protein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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