Structural and Dynamic Implications of an Effector-induced Backbone Amide cis-trans Isomerization in Cytochrome P450cam
DOI
10.1016/j.jmb.2009.03.046
Document Type
Journal Article
Publication Date
5-15-2009
Publication Title
Journal of Molecular Biology
Volume
388
Issue
4
First Page
801
Last Page
814
ISSN
222836
Keywords
electron transfer, molecular dynamics, NMR
Abstract
Experimental evidence has been provided for a functionally relevant cis-trans isomerization of the Ile88-Pro89 peptide bond in cytochrome P450cam (CYP101). The isomerization is proposed to be a key element of the structural reorganization leading to the catalytically competent form of CYP101 upon binding of the effector protein putidaredoxin (Pdx). A detailed comparison of the results of molecular dynamics simulations on the cis and trans conformations of substrate- and carbonmonoxy-bound ferrous CYP101 with sequence-specific Pdx-induced structural perturbations identified by nuclear magnetic resonance is presented, providing insight into the structural and dynamic consequences of the isomerization. The mechanical coupling between the Pdx binding site on the proximal face of CYP101 and the site of isomerization is described. © 2009 Elsevier Ltd. All rights reserved.
Open Access
Green Accepted
Preprint
Repository Citation
Asciutto, E., Madura, J., Pochapsky, S., OuYang, B., & Pochapsky, T. (2009). Structural and Dynamic Implications of an Effector-induced Backbone Amide cis-trans Isomerization in Cytochrome P450cam. Journal of Molecular Biology, 388 (4), 801-814. https://doi.org/10.1016/j.jmb.2009.03.046