title: X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2.
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.
authors.affiliation: Infection and Immunity Program, Biomedicine Discovery Institute, Department of Microbiology, Monash University, Clayton, Victoria, 3800.|CSIRO Manufacturing, Clayton, Victoria, Australia.
authors.forename: Birgit
authors.initials: B
authors.lastname: Unterweger
authors.affiliation: Infection and Immunity Program, Biomedicine Discovery Institute, Department of Microbiology, Monash University, Clayton, Victoria, 3800.
authors.forename: Nyssa
authors.initials: N
authors.lastname: Drinkwater
authors.affiliation: Infection and Immunity Program, Biomedicine Discovery Institute, Department of Microbiology, Monash University, Clayton, Victoria, 3800.
authors.forename: Priscilla
authors.initials: P
authors.lastname: Johanesen
authors.affiliation: Infection and Immunity Program, Biomedicine Discovery Institute, Department of Microbiology, Monash University, Clayton, Victoria, 3800.
authors.forename: Dena
authors.initials: D
authors.lastname: Lyras
authors.affiliation: CSIRO Manufacturing, Clayton, Victoria, Australia.
authors.forename: Geoffrey J
authors.initials: GJ
authors.lastname: Dumsday
authors.affiliation: Infection and Immunity Program, Biomedicine Discovery Institute, Department of Microbiology, Monash University, Clayton, Victoria, 3800.
authors.forename: Sheena
authors.initials: S
authors.lastname: McGowan
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D003511:Cyclohexanols / Q000737:chemistry* / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000077591:Eucalyptol; D015870:Gene Expression; D006900:Hydroxylation; D008958:Models, Molecular; D039821:Monoterpenes / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D042301:Sphingomonadaceae / Q000737:chemistry* / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D003511:Cyclohexanols; D039821:Monoterpenes; D011994:Recombinant Proteins; D003577:Cytochrome P-450 Enzyme System; D000077591:Eucalyptol
keywords: 1,8-cineole; crystallography; cytochrome P450 monooxygenase; hydroxylation