Structural highlights
Publication Abstract from PubMed
The cytochrome P450 monooxygenases (P450s) catalyse a vast array of oxygenation reactions that can be useful in biocatalytic applications. CYP101J2 from Sphingobium yanoikuyae is a P450 that catalyses the hydroxylation of 1,8-cineole. Here we report the crystallisation and X-ray structure elucidation of recombinant CYP101J2 to 1.8 A 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. This article is protected by copyright. All rights reserved.
X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2.,Unterweger B, Drinkwater N, Johanesen P, Lyras D, Dumsday GJ, McGowan S Proteins. 2016 Dec 9. doi: 10.1002/prot.25227. PMID:27936485[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Unterweger B, Drinkwater N, Johanesen P, Lyras D, Dumsday GJ, McGowan S. X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2. Proteins. 2016 Dec 9. doi: 10.1002/prot.25227. PMID:27936485 doi:http://dx.doi.org/10.1002/prot.25227
