1. Comparison of intrinsic dynamics of cytochrome p450 proteins using normal mode analysis
- Author
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Shane W. Hodgson, Mariah E. Dorner, Beatrice R. Soderholm, Christopher A. Monte, Jessica M. Dulli, Justin W. Mabin, Daniel L. Mazula, Shawn W. Keenan, Sanchita Hati, Augustus Olthafer, Cody R. Fisher, Alexander M. Strom, Ryan D. McMunn, Samuel C. Fehling, Ashley E. Sexton, Brecken E. Calhoon, Michelle R. Conlon, Alyssa N. Kruger, and Thomas G. Bartholow
- Subjects
chemistry.chemical_classification ,CYP7B1 ,biology ,Cytochrome b ,Stereochemistry ,Cytochrome P450 reductase ,Cytochrome P450 ,Protein superfamily ,Monooxygenase ,Biochemistry ,chemistry.chemical_compound ,Enzyme ,chemistry ,biology.protein ,Molecular Biology ,Heme - Abstract
Cytochrome P450 enzymes are hemeproteins that catalyze the monooxygenation of a wide-range of structurally diverse substrates of endogenous and exogenous origin. These heme monooxygenases receive electrons from NADH/NADPH via electron transfer proteins. The cytochrome P450 enzymes, which constitute a diverse superfamily of more than 8,700 proteins, share a common tertiary fold but 55% and Bhattacharyya coefficient > 80%), despite the low sequence identity (< 25%) and sequence similarity (< 50%) across the cytochrome P450 superfamily. Noticeable differences in Cα atom fluctuations of structural elements responsible for substrate binding were noticed. These differences in residue fluctuations might be crucial for substrate selectivity in these enzymes.
- Published
- 2015