Conformational dynamics of adenylate kinase in crystals
Category
Published on
Type
journal-article
Author
Junhyung Kim and Sojin Moon and Tod D. Romo and Yifei Yang and Euiyoung Bae and George N. Phillips
Citation
Kim, J., Moon, S., Romo, T. D., Yang, Y., Bae, E., & Phillips, G. N. (2024). Conformational dynamics of adenylate kinase in crystals. Structural Dynamics, 11(1). https://doi.org/10.1063/4.0000205
Abstract
Adenylate kinase is a ubiquitous enzyme in living systems and undergoes dramatic conformational changes during its catalytic cycle. For these reasons, it is widely studied by genetic, biochemical, and biophysical methods, both experimental and theoretical. We have determined the basic crystal structures of three differently liganded states of adenylate kinase from Methanotorrus igneus, a hyperthermophilic organism whose adenylate kinase is a homotrimeric oligomer. The multiple copies of each protomer in the asymmetric unit of the crystal provide a unique opportunity to study the variation in the structure and were further analyzed using advanced crystallographic refinement methods and analysis tools to reveal conformational heterogeneity and, thus, implied dynamic behaviors in the catalytic cycle.
