Investigation of intrinsic dynamics of enzymes involved in metabolic pathways using coarse-grained normal mode analysis
2017
Meeuwsen, Sarah M. | Hodac, An N. | Adams, Lauren M. | McMunn, Ryan D. | Anschutz, Maxwell S. | Carothers, Kari J. | Egdorf, Rachel E. | Hanneman, Peter M. | Kitzrow, Jonathan P. | Keonigsberg, Cynthia K. | Lopez-Martinez, Oscar | Matthew, Paul A. | Richter, Ethan H. | Schenk, Jonathan E. | Schmit, Heidi L. | Scott, Matthew A. | Volenec, Eva M. | Hati, Sanchita | Akhter, Yusuf
Intrinsic dynamics of proteins are known to play important roles in their function. In particular, collective dynamics of a protein, which are defined by the protein’s overall architecture, are important in promoting the active site conformation that favors substrate binding and effective catalysis. The primary sequence of a protein, which determines its three-dimensional structure, encodes unique dynamics. The intrinsic dynamics of a protein actually link protein structure to its function. In the present study, coarse-grained normal mode analysis was performed to examine the intrinsic dynamic patterns of 24 different enzymes involved in primary metabolic pathways. We observed that each metabolic enzyme exhibits unique patterns of motions, which are conserved across multiple species and functionally relevant. Dynamic cross-correlation matrices (DCCMs) are visibly identical for a given enzyme family but significantly different from DCCMs of other protein families, reinforcing that proteins with similar function exhibit a similar pattern of motions. The present work also reasserted that correct identification of unknown proteins is possible based on their intrinsic mobility patterns.
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