Unterweger Birgit, Drinkwater Nyssa, Johanesen Priscilla, Lyras Dena, Dumsday Geoffrey J, McGowan Sheena
Infection and Immunity Program, Biomedicine Discovery Institute, Department of Microbiology, Monash University, Clayton, Victoria, 3800.
CSIRO Manufacturing, Clayton, Victoria, Australia.
Proteins. 2017 May;85(5):945-950. doi: 10.1002/prot.25227. Epub 2017 Mar 3.
The cytochrome P450 monooxygenases (P450s) catalyze a vast array of oxygenation reactions that can be useful in biocatalytic applications. CYP101J2 from Sphingobium yanoikuyae is a P450 that catalyzes the hydroxylation of 1,8-cineole. Here we report the crystallization and X-ray structure elucidation of recombinant CYP101J2 to 1.8 Å resolution. The CYP101J2 structure shows the canonical P450-fold and has an open conformation in the absence of substrate. Analysis of the structure revealed that CYP101J2, in the absence of substrate, forms a well-ordered substrate-binding channel that suggests a unique form of substrate guidance in comparison to other bacterial 1,8-cineole-hydroxylating P450 enzymes. Proteins 2017; 85:945-950. © 2016 Wiley Periodicals, Inc.
细胞色素P450单加氧酶（P450s）催化大量的氧化反应，这些反应在生物催化应用中可能很有用。来自食烷鞘氨醇菌的CYP101J2是一种催化1,8-桉叶素羟基化的P450。在此，我们报告了重组CYP101J2的结晶及分辨率为1.8 Å的X射线晶体结构解析。CYP101J2结构呈现出典型的P450折叠，且在无底物时具有开放构象。对该结构的分析表明，在无底物时，CYP101J2形成了一个有序的底物结合通道，这表明与其他细菌1,8-桉叶素羟基化P450酶相比，它具有独特的底物引导形式。《蛋白质》2017年；85:945 - 950。© 2016威利期刊公司。
