5OMU

Crystal structure of Amycolatopsis cytochrome P450 GcoA in complex with syringol

5OMU の概要

• エントリーDOI: 10.2210/pdb5omu/pdb
• 分子名称: Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, 2,6-dimethoxyphenol, ... (4 entities in total)
• 機能のキーワード: cytochrome, p450, guaiacol, lignin, cyp255a, amycolatopsis, heme, haem, oxidoreductase, syringol
• 由来する生物種: Amycolatopsis sp. ATCC 39116
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46223.42

構造登録者

Mallinson, S.J.B.,Johnson, C.W.,Neidle, E.L.,Beckham, G.T.,McGeehan, J.E. (登録日: 2017-08-01, 公開日: 2018-07-04, 最終更新日: 2024-06-19)

主引用文献

Mallinson, S.J.B.,Machovina, M.M.,Silveira, R.L.,Garcia-Borras, M.,Gallup, N.,Johnson, C.W.,Allen, M.D.,Skaf, M.S.,Crowley, M.F.,Neidle, E.L.,Houk, K.N.,Beckham, G.T.,DuBois, J.L.,McGeehan, J.E.
A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion.
Nat Commun, 9:2487-2487, 2018

PubMed Abstract: Microbial aromatic catabolism offers a promising approach to convert lignin, a vast source of renewable carbon, into useful products. Aryl-O-demethylation is an essential biochemical reaction to ultimately catabolize coniferyl and sinapyl lignin-derived aromatic compounds, and is often a key bottleneck for both native and engineered bioconversion pathways. Here, we report the comprehensive characterization of a promiscuous P450 aryl-O-demethylase, consisting of a cytochrome P450 protein from the family CYP255A (GcoA) and a three-domain reductase (GcoB) that together represent a new two-component P450 class. Though originally described as converting guaiacol to catechol, we show that this system efficiently demethylates both guaiacol and an unexpectedly wide variety of lignin-relevant monomers. Structural, biochemical, and computational studies of this novel two-component system elucidate the mechanism of its broad substrate specificity, presenting it as a new tool for a critical step in biological lignin conversion.

PubMed: 29950589
DOI: 10.1038/s41467-018-04878-2

実験手法

X-RAY DIFFRACTION (1.95 Å)