The crystal structure of P450-TT heme-domain provides the first structural insights into the versatile class VII P450s

DOI: 10.1016/j.bbrc.2018.05.014

Authors: Michele Tavanti (Manchester Institute of Biotechnology (MIB), The University of Manchester) , Joanne L. Porter (Manchester Institute of Biotechnology (MIB), The University of Manchester) , Colin Levy (Manchester Institute of Biotechnology (MIB), The University of Manchester) , Jose Ruben Gomez Castellanos (University of Pavia) , Sabine L. Flitsch (Manchester Institute of Biotechnology (MIB), The University of Manchester) , Nicholas J. Turner (Manchester Institute of Biotechnology (MIB), The University of Manchester)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical And Biophysical Research Communications

State: Published (Approved)
Published: May 2018
Diamond Proposal Number(s): 17773

Abstract: The first crystal structure of a class VII P450, CYP116B46 from Tepidiphilus thermophilus, has been solved at 1.9 Å resolution. The structure reveals overall conservation of the P450-fold and a water conduit around the I-helix. Active site residues have been identified and sequence comparisons have been made with other class VII enzymes. A structure similarity search demonstrated that the P450-TT structure is similar to enzymes capable of oxy-functionalization of fatty acids, terpenes, macrolides, steroids and statins. The insight gained from solving this structure will provide a guideline for future engineering and modelling studies on this catalytically promiscuous class of enzymes.

Journal Keywords: CYP; Biocatalysis; C-H activation; Crystallography; Hydroxylation

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 24/05/2018 09:08

Discipline Tags:

Biochemistry Catalysis Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)