Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.
The bacterial phosphotransferase system (PTS) couples phosphoryl transfer, via a series of bimolecular protein-protein interactions, to sugar transport across the membrane. The multitude of complexes in the PTS provides a paradigm for studying protein interactions, and for understanding how the same binding surface can specifically recognize a diverse array of targets. Fifteen years of work aimed at solving the solution structures of all soluble protein-protein complexes of the PTS has served as a test bed for developing NMR and integrated hybrid approaches to study larger complexes in solution and to probe transient, spectroscopically invisible states, including encounter complexes. We review these approaches, highlighting the problems that can be tackled with these methods, and summarize the current findings on protein interactions.
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA. Electronic address: mariusc@mail.nih.gov.
G Marius
GM
Clore
Vincenzo
V
Venditti
D001419:Bacteria / Q000201:enzymology* / Q000378:metabolism; D003593:Cytoplasm / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation
D010731:Phosphoenolpyruvate Sugar Phosphotransferase System
NMR spectroscopy; bacterial phosphotransferase system; encounter complexes; hybrid methods in structure determination; protein–protein recognition; residual dipolar couplings; signal transduction; solution X-ray scattering; sparsely populated states