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

Abstract

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.

Authors:
 [1];  [1]
  1. National Institute of Health, Bethesda, MD (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
NIH OTHER
OSTI Identifier:
1182781
Resource Type:
Journal Article
Resource Relation:
Journal Name: Trends in Biochemical Sciences; Journal Volume: 38; Journal Issue: 10
Country of Publication:
United States
Language:
ENGLISH
Subject:
signal transduction; protein–protein recognition; bacterial phosphotransferase system; NMR spectroscopy; hybrid methods in structure determination; residual dipolar couplings; solution X-ray scattering; sparsely populated states; encounter complexes

Citation Formats

Clore, G. Marius, and Venditti, Vincenzo. Structure, dynamics and biophysics of the cytoplasmic protein–protein complexes of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system. United States: N. p., 2013. Web. doi:10.1016/j.tibs.2013.08.003.
Clore, G. Marius, & Venditti, Vincenzo. Structure, dynamics and biophysics of the cytoplasmic protein–protein complexes of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system. United States. doi:10.1016/j.tibs.2013.08.003.
Clore, G. Marius, and Venditti, Vincenzo. Tue . "Structure, dynamics and biophysics of the cytoplasmic protein–protein complexes of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system". United States. doi:10.1016/j.tibs.2013.08.003.
@article{osti_1182781,
title = {Structure, dynamics and biophysics of the cytoplasmic protein–protein complexes of the bacterial phosphoenolpyruvate: Sugar phosphotransferase system},
author = {Clore, G. Marius and Venditti, Vincenzo},
abstractNote = {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.},
doi = {10.1016/j.tibs.2013.08.003},
journal = {Trends in Biochemical Sciences},
number = 10,
volume = 38,
place = {United States},
year = {Tue Oct 01 00:00:00 EDT 2013},
month = {Tue Oct 01 00:00:00 EDT 2013}
}