Structural highlights
Publication Abstract from PubMed
The first crystal structure of a class VII P450, CYP116B46 from Tepidiphilus thermophilus, has been solved at 1.9A 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.
The crystal structure of P450-TT heme-domain provides the first structural insights into the versatile class VII P450s.,Tavanti M, Porter JL, Levy CW, Gomez Castellanos JR, Flitsch SL, Turner NJ Biochem Biophys Res Commun. 2018 May 17. pii: S0006-291X(18)31059-3. doi:, 10.1016/j.bbrc.2018.05.014. PMID:29738765[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tavanti M, Porter JL, Levy CW, Gomez Castellanos JR, Flitsch SL, Turner NJ. The crystal structure of P450-TT heme-domain provides the first structural insights into the versatile class VII P450s. Biochem Biophys Res Commun. 2018 May 17. pii: S0006-291X(18)31059-3. doi:, 10.1016/j.bbrc.2018.05.014. PMID:29738765 doi:http://dx.doi.org/10.1016/j.bbrc.2018.05.014
