X‐ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2 |
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| Authors: | Priscilla Johanesen Dena Lyras Geoffrey J. Dumsday Sheena McGowan |
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| Affiliation: | 1. Infection and Immunity Program, Biomedicine Discovery Institute, Department of Microbiology, Monash University, Clayton, Victoria;2. CSIRO Manufacturing, Clayton, Victoria, Australia |
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| Abstract: | 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. |
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| Keywords: | cytochrome P450 monooxygenase 1,8‐cineole hydroxylation crystallography |
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