3O1A

Structure of OxyE (CYP165D3), a Cytochrome P450 Involved in Teicoplanin Biosynthesis

3O1A の概要

• エントリーDOI: 10.2210/pdb3o1a/pdb
• 分子名称: Oxy protein, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: cytochrome p450 fold, phenolic coupling enzyme, tcp12 pcp domain, antibiotic biosynthesis, oxidoreductase
• 由来する生物種: Actinoplanes teichomyceticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47267.76

構造登録者

Cryle, M.J.,Schlichting, I. (登録日: 2010-07-21, 公開日: 2010-11-03, 最終更新日: 2023-09-06)

主引用文献

Cryle, M.J.,Staaden, J.,Schlichting, I.
Structural characterization of CYP165D3, a cytochrome P450 involved in phenolic coupling in teicoplanin biosynthesis.
Arch.Biochem.Biophys., 507:163-173, 2011

PubMed Abstract: Teicoplanin is a glycopeptide antibiotic with activity against Gram-positive bacteria and remains one of the last lines of clinical defense against certain bacterial infections. We have cloned, expressed, and purified the cytochrome P450 OxyE (CYP165D3) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide. The crystal structure of OxyE has been determined to 2.5Å resolution, revealing the probable binding surface for the carrier protein substrate and an extension of the active site into a pocket located above the β-1 sheet. The binding of potential substrates to OxyE shows that peptidyl carrier protein-bound linear peptides bind to OxyE, albeit with low affinity in the absence of a phenolic cross-link that should normally be installed by another Oxy protein in the teicoplanin biosynthetic pathway. This result indicates that the carrier protein alone is not sufficient for tight substrate binding to OxyE and that the Oxy proteins sense the structure of the bound peptide in addition to the presence of the carrier protein, a feature distinct from other carrier protein/P450 systems.

PubMed: 20974107
DOI: 10.1016/j.abb.2010.10.017

実験手法

X-RAY DIFFRACTION (2.5 Å)