Details
| Original language | English |
|---|---|
| Article number | 2464 |
| Number of pages | 13 |
| Journal | Nature Communications |
| Volume | 16 |
| Issue number | 1 |
| Publication status | Published - 12 Mar 2025 |
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.
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
- Biochemistry, Genetics and Molecular Biology(all)
- General Biochemistry,Genetics and Molecular Biology
- Physics and Astronomy(all)
- General Physics and Astronomy
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In: Nature Communications, Vol. 16, No. 1, 2464, 12.03.2025.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Structure and function of the geldanamycin amide synthase from Streptomyces hygroscopicus
AU - Ewert, Wiebke
AU - Bartens, Christian
AU - Ongouta, Jekaterina
AU - Holmes, Monika
AU - Heutling, Anja
AU - Kishore, Anusha
AU - Urbansky, Tim
AU - Zeilinger, Carsten
AU - Preller, Matthias
AU - Kirschning, Andreas
N1 - Publisher Copyright: © The Author(s) 2025.
PY - 2025/3/12
Y1 - 2025/3/12
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=105000075851&partnerID=8YFLogxK
U2 - 10.1038/s41467-025-57013-3
DO - 10.1038/s41467-025-57013-3
M3 - Article
C2 - 40075103
AN - SCOPUS:105000075851
VL - 16
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
M1 - 2464
ER -