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2YOO

Cholest-4-en-3-one bound structure of CYP142 from Mycobacterium smegmatis

2YOO の概要
エントリーDOI10.2210/pdb2yoo/pdb
関連するPDBエントリー4BB8
分子名称P450 HEME-THIOLATE PROTEIN, PROTOPORPHYRIN IX CONTAINING FE, (8ALPHA,9BETA)-CHOLEST-4-EN-3-ONE, ... (5 entities in total)
機能のキーワードoxidoreductase, cholesterol metabolism
由来する生物種Mycobacterium smegmatis str. MC2 155
タンパク質・核酸の鎖数4
化学式量合計187148.85
構造登録者
Garcia-Fernandez, E.,Frank, D.J.,Galan, B.,Kells, P.M.,Podust, L.M.,Garcia, J.L.,Ortiz de Montellano, P.R. (登録日: 2012-10-25, 公開日: 2013-02-27, 最終更新日: 2023-12-20)
主引用文献Garcia-Fernandez, E.,Frank, D.J.,Galan, B.,Kells, P.M.,Podust, L.M.,Garcia, J.L.,Ortiz de Montellano, P.R.
A Highly Conserved Mycobacterial Cholesterol Catabolic Pathway.
Environ.Microbiol., 15:2342-, 2013
Cited by
PubMed Abstract: Degradation of the cholesterol side-chain in Mycobacterium tuberculosis is initiated by two cytochromes P450, CYP125A1 and CYP142A1, that sequentially oxidize C26 to the alcohol, aldehyde and acid metabolites. Here we report characterization of the homologous enzymes CYP125A3 and CYP142A2 from Mycobacterium smegmatis mc(2) 155. Heterologously expressed, purified CYP125A3 and CYP142A2 bound cholesterol, 4-cholesten-3-one, and antifungal azole drugs. CYP125A3 or CYP142A2 reconstituted with spinach ferredoxin and ferredoxin reductase efficiently hydroxylated 4-cholesten-3-one to the C-26 alcohol and subsequently to the acid. The X-ray structures of both substrate-free CYP125A3 and CYP142A2 and of cholest-4-en-3-one-bound CYP142A2 reveal significant differences in the substrate binding sites compared with the homologous M. tuberculosis proteins. Deletion only of cyp125A3 causes a reduction of both the alcohol and acid metabolites and a strong induction of cyp142 at the mRNA and protein levels, indicating that CYP142A2 serves as a functionally redundant back up enzyme for CYP125A3. In contrast to M. tuberculosis, the M. smegmatis Δcyp125Δcyp142 double mutant retains its ability to grow on cholesterol albeit with a diminished capacity, indicating an additional level of redundancy within its genome.
PubMed: 23489718
DOI: 10.1111/1462-2920.12108
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.69 Å)
構造検証レポート
Validation report summary of 2yoo
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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