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Structure of N-myristoyltransferase from Aspergillus fumigatus

Takashi Shimada1, Makoto Suzuki1, Shin-ichi Katakura1

  • 1Drug Discovery and Biomedical Technology Unit, Daiichi Sankyo RD Novare Co. Ltd, 1-16-13 Kita-kasai, Edogawa-ku, Tokyo 134-8630, Japan.

Acta Crystallographica. Section D, Biological Crystallography
|April 8, 2015
PubMed

Insights

N-Myristoyltransferase (NMT) is crucial for protein modification and fungal growth. This study reveals the crystal structure of an NMT-inhibitor complex, aiding antifungal drug design.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Drug Discovery

Background:

  • N-Myristoyltransferase (NMT) facilitates protein myristoylation, a vital post-translational modification in eukaryotes.
  • NMT is essential for the growth of fungi like Saccharomyces cerevisiae, making it a promising antifungal drug target.
  • Understanding NMT structure is key to developing specific inhibitors.

Purpose of the Study:

  • To elucidate the structural basis of N-myristoyltransferase inhibition.
  • To provide insights for the rational design of novel antifungal agents targeting NMT.

Main Methods:

  • X-ray crystallography was employed to determine the structure of a ternary complex.
  • The complex included NMT from Aspergillus fumigatus, a myristoyl-CoA analogue (S-(2-oxo)pentadecyl-CoA), and a synthetic inhibitor.
  • High-resolution data was collected to 2.1 Å.

Main Results:

  • The crystal structure of the Aspergillus fumigatus NMT ternary complex was determined.
  • Detailed structural information on the interaction between NMT, cofactor analogue, and inhibitor was obtained.
  • The findings offer insights into the specificity of NMT inhibitors.

Conclusions:

  • The determined structure advances the understanding of NMT inhibitor specificity.
  • This structural information is valuable for structure-based drug design against fungal pathogens.
  • The study provides a foundation for developing new antifungal therapies targeting NMT.
Keywords:
Aspergillus fumigatusN-myristoyltransferase

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