7E3Z
Non-Ribosomal Peptide Synthetases, Thioesterase
Summary for 7E3Z
| Entry DOI | 10.2210/pdb7e3z/pdb |
| Descriptor | thioesterase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | non-ribosomal peptide synthetases, hydrolase |
| Biological source | Streptomyces sp. SNM55 |
| Total number of polymer chains | 1 |
| Total formula weight | 28673.12 |
| Authors | Jung, Y.E.,Cha, S.S. (deposition date: 2021-02-09, release date: 2021-12-22, Last modification date: 2024-05-29) |
| Primary citation | Kim, M.S.,Bae, M.,Jung, Y.E.,Kim, J.M.,Hwang, S.,Song, M.C.,Ban, Y.H.,Bae, E.S.,Hong, S.,Lee, S.K.,Cha, S.S.,Oh, D.C.,Yoon, Y.J. Unprecedented Noncanonical Features of the Nonlinear Nonribosomal Peptide Synthetase Assembly Line for WS9326A Biosynthesis. Angew.Chem.Int.Ed.Engl., 60:19766-19773, 2021 Cited by PubMed Abstract: Systematic inactivation of nonribosomal peptide synthetase (NRPS) domains and translocation of the thioesterase (TE) domain revealed several unprecedented nonlinear NRPS assembly processes during the biosynthesis of the cyclodepsipeptide WS9326A in Streptomyces sp. SNM55. First, two sets of type ΙΙ TE (TEΙΙ)-like enzymes mediate the shuttling of activated amino acids between two sets of stand-alone adenylation (A)-thiolation (T) didomain modules and an "A-less" condensation (C)-T module with distinctive specificities and flexibilities. This was confirmed by the elucidation of the affinities of the A-T didomains for the TEΙΙs and its structure. Second, the C-T didomain module operates iteratively and independently from other modules in the same protein to catalyze two chain elongation cycles. Third, this biosynthetic pathway includes the first example of module skipping, where the interpolated C and T domains are required for chain transfer. PubMed: 33963654DOI: 10.1002/anie.202103872 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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