6ojd | pdb_00006ojd

A high-resolution crystal structure of covalent complex of NocB thioesterase domain with fluorophosphonate nocardicin G analog

spinqualitylabelsall models 6ojd, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ojd is a 4 chain structure with sequence from "nocardia_uniformis_subsp._tsuyamanensis"_aoki_et_al._1976 "nocardia uniformis subsp. tsuyamanensis" aoki et al. 1976. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GOL, MUY Related: 6ojc Gene: nocB ("Nocardia uniformis subsp. tsuyamanensis" Aoki et al. 1976) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Nonribosomal peptide synthetases (NRPSs) underlie the biosynthesis of many natural products that have important medicinal utility. Protection of the NRPS peptide products from proteolysis is critical to these pathways and is often achieved by structural modification, principally the introduction of D-amino acid residues into the elongating peptide. These amino acids are generally formed in situ from their L-stereoisomers by epimerization domains or dual-function condensation/epimerization domains. In singular contrast, the thioesterase domain of nocardicin biosynthesis mediates both the effectively complete L- to D-epimerization of its C-terminal amino acid residue (>/=100:1) and hydrolytic product release. We report herein high-resolution crystal structures of the nocardicin thioesterase domain in ligand-free form and reacted with a structurally precise fluorophosphonate substrate mimic that identify the complete peptide binding pocket to accommodate both stereoisomers. These structures combined with additional functional studies provide detailed mechanistic insight into this unique dual-function NRPS domain. Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions.,Patel KD, d'Andrea FB, Gaudelli NM, Buller AR, Townsend CA, Gulick AM Nat Commun. 2019 Aug 27;10(1):3868. doi: 10.1038/s41467-019-11740-6. PMID:31455765 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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