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Structure and function of the geldanamycin amide synthase from Streptomyces hygroscopicus

Author

Listed:
  • Wiebke Ewert

    (Hannover Medical School)

  • Christian Bartens

    (Leibniz University Hannover)

  • Jekaterina Ongouta

    (Leibniz University Hannover)

  • Monika Holmes

    (Leibniz University Hannover)

  • Anja Heutling

    (Leibniz University Hannover)

  • Anusha Kishore

    (Center of Biomolecular Drug Research (BMWZ) Leibniz University Hannover)

  • Tim Urbansky

    (University of Applied Sciences Bonn-Rhein-Sieg)

  • Carsten Zeilinger

    (Center of Biomolecular Drug Research (BMWZ) Leibniz University Hannover)

  • Matthias Preller

    (Hannover Medical School
    University of Applied Sciences Bonn-Rhein-Sieg)

  • Andreas Kirschning

    (Leibniz University Hannover
    University Uppsala)

Abstract

Amide synthases catalyze the formation of macrolactam rings from aniline-containing polyketide-derived seco-acids as found in the important class of ansamycin antibiotics. One of these amide synthases is the geldanamycin amide synthase GdmF, which we recombinantly expressed, purified and studied in detail both functionally as well as structurally. Here we show that purified GdmF catalyzes the amide formation using synthetically derived substrates. The atomic structures of the ligand-free enzyme and in complex with simplified substrates reveal distinct structural features of the substrate binding site and a putative role of the flexible interdomain region for the catalysis reaction.

Suggested Citation

  • Wiebke Ewert & Christian Bartens & Jekaterina Ongouta & Monika Holmes & Anja Heutling & Anusha Kishore & Tim Urbansky & Carsten Zeilinger & Matthias Preller & Andreas Kirschning, 2025. "Structure and function of the geldanamycin amide synthase from Streptomyces hygroscopicus," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57013-3
    DOI: 10.1038/s41467-025-57013-3
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