4PWV

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

4PWV の概要

• エントリーDOI: 10.2210/pdb4pwv/pdb
• 関連するPDBエントリー: 4L0E 4L0F 4PXH
• 分子名称: P450 monooxygenase, Peptide synthetase, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: cytochrome p450 fold, beta-aminoacyl carrier protein hydroxylase, peptidyl carrier protein domains, skyllamycin nrps, oxidoreductase-protein binding complex, oxidoreductase/protein binding
• 由来する生物種: Streptomyces sp. Acta 2897; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61046.60

構造登録者

Haslinger, K.,Cryle, M.J. (登録日: 2014-03-21, 公開日: 2014-07-23, 最終更新日: 2024-11-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3 Å)