Have enzyme folds evolved due to the role of protein dynamics in catalysis?

Abstract

An integrated view of protein structure, dynamics and function is emerging, where proteins are considered as dynamically active assemblies and internal motions are closely linked to function such as enzyme catalysis. In the past, enzymes have been viewed as static entities and their high catalytic power has been explained on the basis of direct structural interactions between the enzyme and the substrate. More recently there is wide interest, both from experimental and computational groups, in investigating internal protein motions. Protein motions have been linked to the rate-enhancement achieved by enzymes. Protein residues far away from the active-site and playing dynamical role, in addition to the active-site residues, are conserved across species ranging from bacteria to human for several enzymes including cyclophilin A, dihydrofolate reductase and ribonuclease A.