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

Research output: Contribution to journalArticle

  • External authors:
  • Joanne L. Porter
  • J. Rubén Gómez Castellanos


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.

Bibliographical metadata

Original languageEnglish
Pages (from-to)846-850
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number4
Early online date17 May 2018
Publication statusPublished - 17 May 2018