5dua | pdb_00005dua

First condensation domain of the calcium-dependent antibiotic synthetase in complex with substrate analogue 3a

spinqualitylabelsall models 5dua, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dua is a 2 chain structure with sequence from Strco. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 5FQ, CL Related: 5du9 Gene: SCO3230 (STRCO) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Nonribosomal peptide synthetases (NRPSs) synthesize a vast variety of small molecules, including antibiotics, antitumors, and immunosuppressants. The NRPS condensation (C) domain catalyzes amide bond formation, the central chemical step in nonribosomal peptide synthesis. The catalytic mechanism and substrate determinants of the reaction are under debate. We developed chemical probes to structurally study the NRPS condensation reaction. These substrate analogs become covalently tethered to a cysteine introduced near the active site, to mimic covalent substrate delivery by carrier domains. They are competent substrates in the condensation reaction and behave similarly to native substrates. Co-crystal structures show C domain-substrate interactions, and suggest that the catalytic histidine's principle role is to position the alpha-amino group for nucleophilic attack. Structural insight provided by these co-complexes also allowed us to alter the substrate specificity profile of the reaction with a single point mutation. Chemical Probes Allow Structural Insight into the Condensation Reaction of Nonribosomal Peptide Synthetases.,Bloudoff K, Alonzo DA, Schmeing TM Cell Chem Biol. 2016 Mar 17;23(3):331-9. doi: 10.1016/j.chembiol.2016.02.012. PMID:26991102 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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