| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8293636 | Biochemical and Biophysical Research Communications | 2018 | 8 Pages |
Abstract
In this work, by using a combination of modeling tools, including comparative modeling, docking, all-atom MD and QM/MM methodologies we studied in detail the reaction mechanism of cmaA2, mmaA4, and mmaA1 CMAS and described the molecular determinants that lead to different products. We have modeled the protein-substrate complex structure and determined the free energy pathway for the reaction. The combination of modeling tools at different levels of complexity allows having a complete picture of the CMAS structure-activity relationship.
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Authors
Lucas A. Defelipe, Federico Osman, Marcelo A. Marti, Adrián G. Turjanski,