Structural Basis for Regulation and Specificity of Fructooligosaccharide Import in Streptococcus pneumoniae

Structure. 2017 Jan 3;25(1):79-93. doi: 10.1016/j.str.2016.11.008. Epub 2016 Dec 8.

Abstract

Streptococcus pneumoniae is dependent on carbohydrate uptake for colonization and pathogenesis, and dedicates over a third of its transport systems to their uptake. The ability of the pneumococcus to utilize fructooligosaccharides (FOSs) is attributed to the presence of one of two types of FOS ATP-binding cassette (ABC) transporters. Strains encoding SfuABC are only able to utilize short-chain FOSs, while strains encoding FusABC can utilize both short- and long-chain FOSs. The crystal structures of the substrate-binding protein FusA in its open and closed conformations bound to FOSs, and solution scattering data of SfuA, delineate the structural basis for import of short- and long-chain FOSs. The structure of FusA identifies an EF hand-like calcium-binding motif. This is shown to be essential for translocation of FOSs in FusABC and forms the basis for the definition of a new class of substrate-binding proteins that regulate substrate translocation by calcium.

Keywords: Streptococcus pneumoniae; calcium signaling; carbohydrate ABC transporters; substrate translocation regulation; substrate-binding proteins.

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry*
  • ATP-Binding Cassette Transporters / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Calcium / metabolism*
  • Crystallography, X-Ray
  • EF Hand Motifs
  • Gene Regulatory Networks
  • Models, Molecular
  • Oligosaccharides / metabolism*
  • Protein Binding
  • Protein Conformation
  • Streptococcus pneumoniae / chemistry
  • Streptococcus pneumoniae / metabolism*
  • Substrate Specificity

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Oligosaccharides
  • fructooligosaccharide
  • Calcium