2n6z | pdb_00002n6z

Solution structure of the salicylate-loaded ArCP from yersiniabactin synthetase

spinqualitylabelsall models 2n6z, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n6z is a 1 chain structure with sequence from "bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: 4HJ Related: 2n6y Gene: irp2, y2399, YPO1911 ("Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Nonribosomal peptide synthetases (NRPSs) are microbial enzymes that produce a wealth of important natural products by condensing substrates in an assembly line manner. The proper sequence of substrates is obtained by tethering them to phosphopantetheinyl arms of holo carrier proteins (CPs) via a thioester bond. CPs in holo and substrate-loaded forms visit NRPS catalytic domains in a series of transient interactions. A lack of structural information on substrate-loaded carrier proteins has hindered our understanding of NRPS synthesis. Here, we present the first structure of an NRPS aryl carrier protein loaded with its substrate via a native thioester bond, together with the structure of its holo form. We also present the first quantification of NRPS CP backbone dynamics. Our results indicate that prosthetic moieties in both holo and loaded forms are in contact with the protein core, but they also sample states in which they are disordered and extend in solution. We observe that substrate loading induces a large conformational change in the phosphopantetheinyl arm, thereby modulating surfaces accessible for binding to other domains. Our results are discussed in the context of NRPS domain interactions. Solution Structure of a Nonribosomal Peptide Synthetase Carrier Protein Loaded with Its Substrate Reveals Transient, Well-Defined Contacts.,Goodrich AC, Harden BJ, Frueh DP J Am Chem Soc. 2015 Sep 23;137(37):12100-9. doi: 10.1021/jacs.5b07772. Epub 2015 , Sep 15. PMID:26334259 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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