The crystal structure of P450-TT heme-domain provides the first structural insights into the versatile class VII P450s
- Manchester Institute of Biotechnology (MIB), School of Chemistry, The University of Manchester, 131Princess Street, M1 7DN, Manchester (United Kingdom)
- Department of Biology and Biotechnology “Lazzaro Spallanzani”, University of Pavia, Via Ferrata 9, 27100, Pavia (Italy)
Highlights: • The crystal structure of CYP116B45 (P450-TT) from T. thermophilus has been solved. • P450-TT crystal structure is the first example of a class VII P450 structure. • P450-TT adopts the typical P450-fold. • Structural deviation of regions involved in substrate recognition is observed. • Analysis of 96 class VII sequences revealed conservation of active site residues. 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.
- OSTI ID:
- 23136994
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 501, Issue 4; Other Information: Copyright (c) 2018 Elsevier Inc. All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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