Darstellung der Elektronendichte an der ausgebildeten Disulfidbrücke (gelb, zwischen C56 und C163) und in deren Nachbarschaft.

Insights into closed enzymes

Scientists at the University of Konstanz and Umeå University in Sweden have arrived at a structural model of the enzyme adenylate kinase in its closed state

The adenylate kinase enzyme is crucial to managing the energy budget of cells, accelerating the biochemical process whereby energy is stored or released. The enzyme continuously changes between open and closed states. In its closed form, adenylate kinase is particularly active biochemically and thus able to accelerate the chemical reaction of “docked” molecules that it has encased like a clam. These are called ligands. Researchers at the Universities of Konstanz (Germany) and Umeå (Sweden) have managed to generate a structural model of the atomic make-up of the enzyme in its closed state, including an embedded ligand. Using nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography, structural information about the enzyme in its closed state was won – information, that is, about the precise moment that the enzyme is biochemically particularly active. A particular trick was necessary to facilitate the structural analysis of the enzyme’s closed state in the first place. The research findings, which provide important information about the biochemical mechanisms that govern the energy budgets of cells, were published in the Journal Proceedings of the National Academy of Sciences (PNAS). Read more...