4pxh | pdb_00004pxh

Structure of P450sky (CYP163B3), a cytochrome P450 from skyllamycin biosynthesis in complex with a peptidyl carrier protein domain

spinqualitylabelsall models 4pxh, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pxh is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM, KH4 Related: 4l0e, 4l0f, 4pwv Activity: Unspecific monooxygenase, with EC number 1.14.14.1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Studying the interplay between nonribosomal peptide synthetases (NRPS), a major source of secondary metabolites, and crucial external modifying enzymes is a challenging task since the interactions involved are often transient in nature. By applying a range of synthetic inhibitor-type compounds, a stabilized complex appropriate for structural analysis was generated for such a tailoring enzyme and an NRPS domain. The complex studied comprises an NRPS peptidyl carrier protein (PCP) domain bound to the Cytochrome P450 enzyme that is crucial for the provision of beta-hydroxylated amino acid precursors in the biosynthesis of the cyclic depsipeptide skyllamycin. The structure reveals that complex formation is governed by hydrophobic interactions, the presence of which can be controlled through minor alterations in PCP structure that enable selectivity amongst multiple highly similar PCP domains. The structure of a transient complex of a nonribosomal Peptide synthetase and a cytochrome p450 monooxygenase.,Haslinger K, Brieke C, Uhlmann S, Sieverling L, Sussmuth RD, Cryle MJ Angew Chem Int Ed Engl. 2014 Aug 4;53(32):8518-22. doi: 10.1002/anie.201404977., Epub 2014 Jul 9. PMID:25044735 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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