From the Manchester Institute of Biotechnology, Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdom
J Biol Chem. 2018 Dec 14;293(50):19211-19212. doi: 10.1074/jbc.H118.006715.
The cytochromes P450 (CYPs) oxidatively transform a huge number of substrates in both prokaryotic and eukaryotic organisms, but the mechanisms by which they accommodate these diverse molecules remain unclear. A new study by Bart and Scott reports two co-crystal structures of CYP1A1 that reveal structural rearrangements and flexible interaction networks that explain how the active site cavity shapes itself around new ligands. These data open the door to an increased understanding of fundamental enzyme behavior and improved searches for anti-cancer compounds.
细胞色素 P450(CYPs)氧化转化了原核和真核生物中大量的底物,但它们适应这些不同分子的机制仍不清楚。Bart 和 Scott 的一项新研究报告了 CYP1A1 的两个共晶结构,揭示了结构重排和灵活的相互作用网络,解释了活性位点腔如何围绕新配体自我塑造。这些数据为深入了解基本酶的行为和改进抗癌化合物的搜索打开了大门。