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Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
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Glycan recognition by the Bacteroidetes Sus-like systems.

David N Bolam1, Nicole M Koropatkin

  • 1Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom.

Current Opinion in Structural Biology
|July 24, 2012
PubMed
Summary

Bacteroidetes use Sus-like systems to break down sugars. Structural studies reveal how surface SusD proteins bind sugars and how hybrid two-component systems (HTCS) sense them for nutrient uptake.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Human gut Bacteroidetes utilize Sus-like systems for glycan acquisition and degradation.
  • Understanding these systems is crucial for comprehending gut microbiome function and host-microbe interactions.

Purpose of the Study:

  • To elucidate the structural basis of glycan binding and sensing mechanisms in Bacteroidetes.
  • To provide insights into the function of SusD proteins and hybrid two-component systems (HTCS).

Main Methods:

  • X-ray crystallography was employed to determine the structures of key proteins.
  • Structural analysis focused on surface-located SusD proteins and periplasmic sensor domains of HTCS.

Main Results:

  • Structures of glycan-binding SusD proteins revealed their role in capturing sugars at the cell surface.
  • Structures of HTCS sensor domains showed two distinct folds, suggesting novel signal transduction mechanisms.
  • Glycan binding to HTCS sensors indicates a unique pathway for regulating gene expression.

Conclusions:

  • The solved structures offer a detailed molecular understanding of glycan utilization by Bacteroidetes.
  • The findings suggest that glycan sensing via HTCS in these bacteria differs from classical two-component systems.