5du9

First condensation domain of the calcium-dependent antibiotic synthetase in complex with substrate analogue 2a

spinqualitylabelsall models 5du9, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5du9 is a 2 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CL, SO4, UM2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9Z4X6_STRCO 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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