4zxi | pdb_00004zxi

Crystal Structure of holo-AB3403 a four domain nonribosomal peptide synthetase bound to AMP and Glycine

spinqualitylabelsall models 4zxi, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zxi is a 1 chain structure with sequence from Acinetobacter baumannii AB307-0294. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: AMP, GLY, MG, NI, PNS, XP4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0X1KH98_ACIB3 Publication Abstract from PubMed Many important natural products are produced by multidomain non-ribosomal peptide synthetases (NRPSs). During synthesis, intermediates are covalently bound to integrated carrier domains and transported to neighbouring catalytic domains in an assembly line fashion. Understanding the structural basis for catalysis with non-ribosomal peptide synthetases will facilitate bioengineering to create novel products. Here we describe the structures of two different holo-non-ribosomal peptide synthetase modules, each revealing a distinct step in the catalytic cycle. One structure depicts the carrier domain cofactor bound to the peptide bond-forming condensation domain, whereas a second structure captures the installation of the amino acid onto the cofactor within the adenylation domain. These structures demonstrate that a conformational change within the adenylation domain guides transfer of intermediates between domains. Furthermore, one structure shows that the condensation and adenylation domains simultaneously adopt their catalytic conformations, increasing the overall efficiency in a revised structural cycle. These structures and the single-particle electron microscopy analysis demonstrate a highly dynamic domain architecture and provide the foundation for understanding the structural mechanisms that could enable engineering of novel non-ribosomal peptide synthetases. Structures of two distinct conformations of holo-non-ribosomal peptide synthetases.,Drake EJ, Miller BR, Shi C, Tarrasch JT, Sundlov JA, Allen CL, Skiniotis G, Aldrich CC, Gulick AM Nature. 2016 Jan 14;529(7585):235-8. doi: 10.1038/nature16163. PMID:26762461 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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