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Crystal structure of full-length CYP116B46 from Tepidiphilus thermophilusCrystal structure of full-length CYP116B46 from Tepidiphilus thermophilus
Structural highlights
FunctionPublication Abstract from PubMedCytochrome P450 monooxygenases are versatile heme-thiolate enzymes that catalyze a wide range of reactions. Self-sufficient cytochrome P450 enzymes contain the redox partners in a single polypeptide chain. Here, we present the crystal structure of full-length CYP116B46, a self-sufficient P450. The continuous polypeptide chain comprises three functional domains, which align well with the direction of electrons traveling from FMN to the heme through the [2Fe-2S] cluster. FMN and the [2Fe-2S] cluster are positioned closely, which facilitates efficient electron shuttling. The edge-to-edge straight-line distance between the [2Fe-2S] cluster and heme is approx. 25.3 A. The role of several residues located between the [2Fe-2S] cluster and heme in the catalytic reaction is probed in mutagenesis experiments. These findings not only provide insights into the intramolecular electron transfer of self-sufficient P450s, but are also of interest for biotechnological applications of self-sufficient P450s. Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.,Zhang L, Xie Z, Liu Z, Zhou S, Ma L, Liu W, Huang JW, Ko TP, Li X, Hu Y, Min J, Yu X, Guo RT, Chen CC Nat Commun. 2020 May 29;11(1):2676. doi: 10.1038/s41467-020-16500-5. PMID:32472090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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