4.6 Article

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

期刊

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2018.05.014

关键词

CYP; Biocatalysis; C-H activation; Crystallography; Hydroxylation

资金

  1. European Union's Seventh Framework Programme for research, technological development and demonstration [613849]
  2. European Union's Horizon 2020 Programme for research and innovation actions [H2020-LEIT BIO-2014-1, 635734]
  3. BBSRC [BB/M017702/1] Funding Source: UKRI

向作者/读者索取更多资源

The first crystal structure of a class VII P450, CYP1161346 from Tepidiphilus thermophilus, has been solved at 1.9 angstrom 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. (C) 2018 Elsevier Inc. All rights reserved.

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