4YT3

CYP106A2

4YT3 の概要

• エントリーDOI: 10.2210/pdb4yt3/pdb
• 関連するPDBエントリー: 4XZO
• 分子名称: Cytochrome P450(MEG), PROTOPORPHYRIN IX CONTAINING FE, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: mono-oxygenase, cytochrome p450, 15-beta-hydroxylase, oxidoreductase
• 由来する生物種: Bacillus megaterium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95382.02

構造登録者

janocha, S.,carius, y.,bernhardt, r.,lancaster, c.r.d. (登録日: 2015-03-17, 公開日: 2016-02-24, 最終更新日: 2024-01-10)

主引用文献

Janocha, S.,Carius, Y.,Hutter, M.,Lancaster, C.R.,Bernhardt, R.
Crystal Structure of CYP106A2 in Substrate-Free and Substrate-Bound Form.
Chembiochem, 17:852-860, 2016

PubMed Abstract: CYP106A2 from Bacillus megaterium ATCC 13368 is known as a bacterial steroid hydroxylase that is also capable of hydroxylating a variety of terpenoids. To analyze the substrate specificity of this enzyme further, different resin acids of the abietane and pimarane types were tested with regard to binding and conversion. Product formation could be shown for all tested substrates. Spectroscopic studies revealed type I binding spectra for isopimaric acid, but dehydroabietic acid did not induce a high-spin shift of the enzyme. Interestingly, binding of abietic acid resulted in a type II difference spectrum typical for nitrogenous inhibitors. Co-crystallization of CYP106A2 with abietic acid and structure determination revealed bending of the heme cofactor when abietic acid was bound in the active site. Quantum chemical calculations strongly suggest that this heme distortion is the cause of the unusual spectroscopic characteristics.

PubMed: 26864272
DOI: 10.1002/cbic.201500524

実験手法

X-RAY DIFFRACTION (1.8 Å)