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Structure of the fucose mutarotase from Streptococcus pneumoniae in complex with L-fucose

Melanie A Higgins1, Alisdair B Boraston

  • 1Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
|December 6, 2011
PubMed

Insights

Streptococcus pneumoniae uses fucose mutarotase (SpFcsU) to convert β-L-fucose to α-L-fucose, aiding its colonization and virulence. This structural study reveals SpFcsU

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Streptococcus pneumoniae utilizes carbohydrate metabolism for host colonization and virulence.
  • The fucose-utilization pathway is crucial for S. pneumoniae's pathogenic mechanisms.
  • Fucose mutarotase (SpFcsU) is a key enzyme in this pathway, catalyzing the interconversion of α-L-fucose and β-L-fucose.

Purpose of the Study:

  • To determine the three-dimensional structure of Streptococcus pneumoniae fucose mutarotase (SpFcsU).
  • To elucidate the structural basis for SpFcsU's enzymatic activity and its role in the fucose-utilization pathway.

Main Methods:

  • Crystallization of SpFcsU in complex with L-fucose.
  • Solving the three-dimensional structure of the SpFcsU-L-fucose complex using X-ray crystallography.

Main Results:

  • The determined structure reveals a decameric quaternary structure for SpFcsU.
  • SpFcsU exhibits high structural similarity to Escherichia coli FcsU (EcFcsU), particularly in the active site.
  • SpFcsU acts as a crucial link in the fucose-utilization pathway, facilitating the conversion of β-fucose to α-fucose.

Conclusions:

  • The structural insights into SpFcsU provide a deeper understanding of fucose metabolism in S. pneumoniae.
  • SpFcsU's structure and function are conserved across different bacterial species, highlighting its importance.
  • Targeting SpFcsU could potentially disrupt S. pneumoniae colonization and virulence.

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