7e3z

Non-Ribosomal Peptide Synthetases, Thioesterase

spinqualitylabelsall models 7e3z, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 IotaIota TE (TEIotaIota)-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 TEIotaIotas 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. Unprecedented Noncanonical Features of the Nonlinear Nonribosomal Peptide Synthetase Assembly Line for WS9326A Biosynthesis.,Kim MS, Bae M, Jung YE, Kim JM, Hwang S, Song MC, Ban YH, Bae ES, Hong S, Lee SK, Cha SS, Oh DC, Yoon YJ Angew Chem Int Ed Engl. 2021 Sep 1;60(36):19766-19773. doi:, 10.1002/anie.202103872. Epub 2021 Jun 17. PMID:33963654 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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