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. 2022 Sep 28;12:16232. doi: 10.1038/s41598-022-20671-0

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Substrate-induced conformational switch is similar in bacterial and eukaryotic CYP51s. Overlaid structures of substrate-bound (grey) and substrate-free (khaki) CYP51 orthologs. M. capsulatus (7SNM and 6MI0, respectively, rmsd of Cα of 2.44 Å), human (6UEZ and 4UHI, rmsd of Cα of 1.98 Å), and T. cruzi (6FMO, molecules A and D, rmsd of Cα of 1.83 Å). The orientation is about the same (upper P450 view). The directions of the changes are outlined with blue arrows on the M. capsulatus CYP51 structure. The carbon atoms of lanosterol (M. capsulatus and human) and obtusifoliol (I105F T. cruzi) are colored in cyan. The ribbons of the parts of the molecules that are not involved in the conserved conformational change^20,21 (7SNM: rmsd of Cα of 0.77) are transparent. For comparison, the ligand-free and detergent-bound M. capsulatus CYP51 structures (6MI0 vs. 6MCW) have RMSD of Cα of 0.37 Å.