X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2

Birgit Unterweger, Nyssa Drinkwater, Priscilla Johanesen, Dena Lyras, Geoffrey J. Dumsday, Sheena McGowan

Research output: Contribution to journalArticleResearchpeer-review

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. 

Original languageEnglish
Pages (from-to)945-950
Number of pages6
JournalProteins: Structure, Function and Bioinformatics
Volume85
Issue number5
DOIs
Publication statusPublished - 1 May 2017

Keywords

  • 1,8-cineole
  • crystallography
  • cytochrome P450 monooxygenase
  • hydroxylation

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