Structural basis for ligand binding to an enzyme by a conformational selection pathway

• DOI: 10.1073/pnas.1700919114
• Publication Date: 2017-05-31T00:40:24Z
• Authors: Michael Kovermann; Christin Grundström; A. Elisabeth Saue...; Uwe H. Sauer; Magnus Wolf-Watz
• Keywords: Energy landscape

Significance Cellular chemical reactions are slow, and to make them compatible with biological life, enzymes have evolved accelerate their associated rate constants. Enzymatic catalysis is a complex process where the increase of constants predominantly depends on reduction free energy barrier for product formation. It now established that transient, so-called high-energy, enzyme states indispensable entities contribute lowering barriers. Such inherently difficult study. Here, we been able arrest catalytically high-energy state adenylate kinase. A detailed characterization its structure, dynamics, function has revealed several aspects together understanding how can perform spectacular function.