6LDL

Crystal structure of CYP116B46-N(20-445) from Tepidiphilus thermophilus in complex with HEME

Summary for 6LDL

• Entry DOI: 10.2210/pdb6ldl/pdb
• Descriptor: Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, BICINE, ... (5 entities in total)
• Functional Keywords: antibiotics, biosynthesis, p450, oxidoreductase
• Biological source: Tepidiphilus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 50292.57

Authors

Zhang, L.L.,Xie, Z.Z.,Huang, J.W.,Liu, W.D.,Chen, C.C.,Guo, R.T. (deposition date: 2019-11-21, release date: 2020-10-28, Last modification date: 2023-11-22)

Primary citation

Zhang, L.,Xie, Z.,Liu, Z.,Zhou, S.,Ma, L.,Liu, W.,Huang, J.W.,Ko, T.P.,Li, X.,Hu, Y.,Min, J.,Yu, X.,Guo, R.T.,Chen, C.C.
Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.
Nat Commun, 11:2676-2676, 2020

PubMed Abstract: Cytochrome 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 Å. 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.

PubMed: 32472090
DOI: 10.1038/s41467-020-16500-5

Experimental method

X-RAY DIFFRACTION (1.38 Å)