8OOM
Structural and functional studies of geldanamycin amide synthase ShGdmF
Summary for 8OOM
| Entry DOI | 10.2210/pdb8oom/pdb |
| Descriptor | GdmF, (2R)-2,4-dihydroxy-3,3-dimethyl-N-{3-oxo-3-[(2-sulfanylethyl)amino]propyl}butanamide, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | amide synthase, geldanamycin, amidase, alpha-beta, biosynthetic protein |
| Biological source | Streptomyces hygroscopicus |
| Total number of polymer chains | 1 |
| Total formula weight | 30312.96 |
| Authors | Ewert, W.,Zeilinger, C.,Kirschning, A.,Preller, M. (deposition date: 2023-04-05, release date: 2024-04-17, Last modification date: 2025-04-02) |
| Primary citation | Ewert, W.,Bartens, C.,Ongouta, J.,Holmes, M.,Heutling, A.,Kishore, A.,Urbansky, T.,Zeilinger, C.,Preller, M.,Kirschning, A. Structure and function of the geldanamycin amide synthase from Streptomyces hygroscopicus. Nat Commun, 16:2464-2464, 2025 Cited by PubMed 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. PubMed: 40075103DOI: 10.1038/s41467-025-57013-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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