5KYO

Crystal Structure of CYP101J2

Summary for 5KYO

• Entry DOI: 10.2210/pdb5kyo/pdb
• Descriptor: CYP101J2, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: cytochrome p450 monooxygenase, 1, 8-cineole hydroxylation, oxidoreductase
• Biological source: Sphingobium yanoikuyae
• Total number of polymer chains: 6
• Total formula weight: 296245.07

Authors

Unterweger, B.,Drinkwater, N.,Dumsday, G.J.,McGowan, S. (deposition date: 2016-07-22, release date: 2017-01-04, Last modification date: 2023-10-04)

Primary citation

Unterweger, B.,Drinkwater, N.,Johanesen, P.,Lyras, D.,Dumsday, G.J.,McGowan, S.
X-ray crystal structure of cytochrome P450 monooxygenase CYP101J2 from Sphingobium yanoikuyae strain B2.
Proteins, 85:945-950, 2017

PubMed 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.

PubMed: 27936485
DOI: 10.1002/prot.25227

Experimental method

X-RAY DIFFRACTION (1.8 Å)