9CJG

P450-G9 from Actinokineospora terrae, a non-canonical, serine-ligated cytochrome P450 in the ligand-free, closed conformation

9CJG の概要

• エントリーDOI: 10.2210/pdb9cjg/pdb
• 分子名称: Cytochrome P450-G9, PROTOPORPHYRIN IX CONTAINING FE, FORMIC ACID, ... (5 entities in total)
• 機能のキーワード: p450, cytochrome, serine, p411, oxidoreductase
• 由来する生物種: Actinokineospora terrae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90331.68

構造登録者

Ireland, K.A.,Davis, K.M. (登録日: 2024-07-06, 公開日: 2025-03-12)

主引用文献

Nguy, A.K.L.,Ireland, K.A.,Kayrouz, C.M.,Caceres, J.C.,Greene, B.L.,Davis, K.M.,Seyedsayamdost, M.R.
Non-Canonical Cytochrome P450 Enzymes in Nature.
Biorxiv, 2024

PubMed Abstract: Cytochrome P450s (CYPs) are a superfamily of thiolate-ligated heme metalloenzymes principally responsible for the hydroxylation of unactivated C-H bonds. The lower-axial cysteine is an obligatory and universally conserved residue for the CYP enzyme class. Herein, we challenge this paradigm by systematically identifying non-canonical CYPs (ncCYPs) that do not harbor a cysteine ligand. Our bioinformatic search reveals 20 distinct ncCYP families with diverse ligands encoded in microbial genomes. We characterize a native serine-ligated CYP with a high-spin ferric resting state. Its crystal structure clearly shows a typical CYP fold and a serine alkoxide as a lower axial heme ligand. In addition, we report the discovery and characterization of the first native selenocysteine-ligated CYP in nature. Our findings radically expand the CYP metalloenzyme family.

PubMed: 39763895
DOI: 10.1101/2024.12.22.630014

実験手法

X-RAY DIFFRACTION (1.85 Å)