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Related Experiment Videos

An enzyme-substrate complex involved in bacterial cell wall biosynthesis

T E Benson1, D J Filman, C T Walsh

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.

Nature Structural Biology
|August 1, 1995
PubMed
Summary

The crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase was determined, revealing a novel flavin binding motif. This finding aids in designing new antibacterial agents targeting bacterial cell wall synthesis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Medicinal Chemistry

Background:

  • UDP-N-acetylenolpyruvylglucosamine reductase is crucial for bacterial cell wall biosynthesis.
  • UDP-N-acetylmuramic acid is a key component of bacterial cell walls.
  • Targeting this enzyme offers a potential strategy for developing novel antibacterial agents.

Purpose of the Study:

  • To determine the crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase.
  • To elucidate the enzyme's substrate-binding and catalytic mechanisms.
  • To provide insights for the rational design of antibacterial drugs.

Main Methods:

  • X-ray crystallography was used to solve the enzyme's structure.
  • The crystal structure was determined to 2.7 Å resolution.

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  • The structure was analyzed in the presence of its substrate, enolpyruvyl-UDP-N-acetylglucosamine.

    • Main Results:

    • The crystal structure revealed a novel flavin binding motif.
    • A striking alignment between the flavin cofactor and the substrate was observed.
    • The structural data suggest a catalytic mechanism for the reduction of the enol ether substrate.

    Conclusions:

    • The determined structure provides a detailed molecular understanding of UDP-N-acetylenolpyruvylglucosamine reductase.
    • The novel flavin binding motif and substrate alignment offer new avenues for drug design.
    • This research contributes to the development of antibacterial agents targeting essential bacterial pathways.