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Structural basis for outer membrane sugar uptake in pseudomonads.

Bert van den Berg1

  • 1Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA. bert.vandenberg@umassmed.edu

The Journal of Biological Chemistry
|October 16, 2012
PubMed
Summary
This summary is machine-generated.

Outer membrane OprB channels in Pseudomonas transport sugars. The crystal structure reveals a unique constriction mechanism, explaining OprB

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Published on: July 4, 2016

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Gram-negative bacteria utilize outer membrane channels for nutrient uptake.
  • Enterobacterial sugar uptake channels like E. coli LamB are well-studied.
  • Pseudomonad sugar uptake relies on OprB channels, with limited mechanistic understanding.

Purpose of the Study:

  • To elucidate the structural basis of OprB-mediated sugar transport.
  • To determine the substrate specificity of OprB channels.

Main Methods:

  • X-ray crystallography of Pseudomonas putida F1 OprB channel.
  • Liposome swelling assays to assess transport kinetics.

Main Results:

  • Determined the crystal structure of a monomeric, 16-stranded beta-barrel OprB channel.
  • Identified conserved arginine and glutamate residues forming a constriction site.
  • Demonstrated OprB's preference for monosaccharides over disaccharides.
  • Observed substrate charge-based selectivity, disfavoring negatively charged molecules.

Conclusions:

  • The OprB channel architecture, particularly the constriction, dictates monosaccharide specificity.
  • OprB's structure differs from LamB, explaining distinct substrate preferences.
  • This study provides a structural framework for understanding OprB function in Pseudomonas.