4PWV

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

Summary for 4PWV

• Entry DOI: 10.2210/pdb4pwv/pdb
• Related: 4L0E 4L0F 4PXH
• Descriptor: P450 monooxygenase, Peptide synthetase, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: cytochrome p450 fold, beta-aminoacyl carrier protein hydroxylase, peptidyl carrier protein domains, skyllamycin nrps, oxidoreductase-protein binding complex, oxidoreductase/protein binding
• Biological source: Streptomyces sp. Acta 2897; More
• Total number of polymer chains: 2
• Total formula weight: 61046.60

Authors

Haslinger, K.,Cryle, M.J. (deposition date: 2014-03-21, release date: 2014-07-23, Last modification date: 2014-08-20)

Primary citation

Haslinger, K.,Brieke, C.,Uhlmann, S.,Sieverling, L.,Sussmuth, R.D.,Cryle, M.J.
The structure of a transient complex of a nonribosomal Peptide synthetase and a cytochrome p450 monooxygenase.
Angew.Chem.Int.Ed.Engl., 53:8518-8522, 2014

PubMed Abstract: 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 β-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.

PubMed: 25044735
DOI: 10.1002/anie.201404977

Experimental method

X-RAY DIFFRACTION (3 Å)