8qrx

Solution NMR structure of the peptidyl carrier domain TomAPCP from the Tomaymycin non-ribosomal peptide synthetase in its substrate-loaded state

spinqualitylabelsall models 8qrx Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8qrx is a 1 chain structure with sequence from Streptomyces regensis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: WP9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed In the quest for new bioactive substances, nonribosomal peptide synthetases (NRPS) provide biodiversity by synthesizing nonproteinaceous peptides with high cellular activity. NRPS machinery consists of multiple modules, each catalyzing a unique series of chemical reactions. Incomplete understanding of the biophysical principles orchestrating these reaction arrays limits the exploitation of NRPSs in synthetic biology. Here, we use nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry to solve the conundrum of how intermodular recognition is coupled with loaded carrier protein specificity in the tomaymycin NRPS. We discover an adaptor domain that directly recruits the loaded carrier protein from the initiation module to the elongation module and reveal its mechanism of action. The adaptor domain of the type found here has specificity rules that could potentially be exploited in the design of engineered NRPS machinery. The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.,Karanth MN, Kirkpatrick JP, Krausze J, Schmelz S, Scrima A, Carlomagno T Sci Adv. 2024 Jun 21;10(25):eadm9404. doi: 10.1126/sciadv.adm9404. Epub 2024 Jun , 19. PMID:38896613 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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