Journal or Book Title
Proceedings of the National Academy of Sciences of the United States of America
The bacterial phosphotransferase system couples phosphoryl transfer to sugar transport across the cell membrane. The first protein in the pathway, Enzyme I (EI), undergoes two large rigid body domain reorientations between an autophosphorylation-competent closed state and an open state that allows subsequent phosphoryl transfer to its downstream protein partner. Simultaneous use of solution X-ray scattering and NMR dipolar coupling data to guide simulated annealing refinement reveals the existence of a dynamic equilibrium between closed and partially closed conformations in a complex of a mutant of EI with phosphoenolpyruvate. The partially closed conformation represents an intermediate in the open-to-closed transition.
Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.
Venditti, Vincenzo; Schwieters, Charles D.; Grishaev, Alexander; and Clore, G. Marius, "Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering" (2015). Chemistry Publications. 107.