Structure, dynamics and biophysics of the cytoplasmic protein–protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system

Abstract

Summary 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.

Hybrid Approaches to Structural Characterization of Conformational Ensembles of Complex Macromolecular Systems Combining NMR Residual Dipolar Couplings and Solution X-ray Scattering

“…EI is responsible for both activation and regulation of the overall PTS. 19,154,155 EI is a large, dynamic protein that presented a real challenge to structural biologists. In this section we will analyze how only the integrated analysis of data from multiple techniques allowed for characterization of the structure and dynamics of EI.…”

A Metabolic Widget Adjusts the Phosphoenolpyruvate-Dependent Fructose Influx in Pseudomonas putida

“…The source of the high-energy phosphate residue that fuels the activity of both PTS systems is PEP (37). Since the source of such a phosphate residue needed for the conversion of Fru into F1P is PEP (12), and considering that this metabolite can be generated from GA3P only under glycolytic conditions (i.e., using either Glu or Fru as the carbon source) (38), the interplay between carbon fluxes and the availability of high-energy phosphate residues was also considered in our interpretation.…”

Profile of Marius Clore

“…For instance, the bacterial phosphotransferase system, which uses biomolecular protein-protein interactions to control the transport of sugars across the bacterial membrane, has provided Clore a platform with which to study how signal transduction proteins recognize structurally dissimilar proteins (10). In addition, his laboratory's role in developing NMR technology for detecting sparsely populated protein states has provided new insights into the biochemistry and interactions of biological macromolecules, and earned him the 2013 Biochemical Society Centenary Award (11).…”