[2024] Conformational dynamics of adenylate kinase in crystals
Journal
Structural Dynamics 2024; 11 (1): 014702
Authors
Kim, J., Moon, S., Romo, T.D., Yang, Y., Bae, E.*, Phillips, G.N.*
*Denotes Corresponding Author
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.
Download link
https://doi.org/10.1063/4.0000205
Journal
Structural Dynamics 2024; 11 (1): 014702
Authors
Kim, J., Moon, S., Romo, T.D., Yang, Y., Bae, E.*, Phillips, G.N.*
*Denotes Corresponding Author
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.
Download link
https://doi.org/10.1063/4.0000205