HADDOCK: a protein− protein docking approach based on biochemical or biophysical information
C Dominguez, R Boelens… - Journal of the American …, 2003 - ACS Publications
The structure determination of protein− protein complexes is a rather tedious and lengthy
process, by both NMR and X-ray crystallography. Several methods based on docking to …
process, by both NMR and X-ray crystallography. Several methods based on docking to …
Histidine phosphorylation in biological systems
J Puttick, EN Baker, LTJ Delbaere - … et Biophysica Acta (BBA)-Proteins and …, 2008 - Elsevier
Histidine phosphorylation is important in prokaryotes and occurs to the extent of 6% of total
phosphorylation in eukaryotes. Nevertheless phosphohistidine residues are not normally …
phosphorylation in eukaryotes. Nevertheless phosphohistidine residues are not normally …
Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system
GT Robillard, J Broos - Biochimica et Biophysica Acta (BBA)-Reviews on …, 1999 - Elsevier
The phosphoenolpyruvate-dependent carbohydrate transport system is responsible for the
transport of a variety of carbohydrates in prokaryotes at the expense of …
transport of a variety of carbohydrates in prokaryotes at the expense of …
Prediction of protein conformational freedom from distance constraints
BL de Groot, DMF Van Aalten… - Proteins: Structure …, 1997 - Wiley Online Library
A method is presented that generates random protein structures that fulfil a set of upper and
lower interatomic distance limits. These limits depend on distances measured in …
lower interatomic distance limits. These limits depend on distances measured in …
Cell signaling, post-translational protein modifications and NMR spectroscopy
FX Theillet, C Smet-Nocca, S Liokatis… - Journal of biomolecular …, 2012 - Springer
Post-translationally modified proteins make up the majority of the proteome and establish, to
a large part, the impressive level of functional diversity in higher, multi-cellular organisms …
a large part, the impressive level of functional diversity in higher, multi-cellular organisms …
Identification by NMR of the Binding Surface for the Histidine-Containing Phosphocarrier Protein HPr on the N-Terminal Domain of Enzyme I of the Escherichia coli …
The interaction between the∼ 30 kDa N-terminal domain of enzyme I (EIN) and the∼ 9.5
kDa histidine-containing phosphocarrier protein HPr of the Escherichia coli …
kDa histidine-containing phosphocarrier protein HPr of the Escherichia coli …
Evidence of link between quorum sensing and sugar metabolism in Escherichia coli revealed via cocrystal structures of LsrK and HPr
Quorum sensing (QS), a bacterial process that regulates population-scale behavior, is
mediated by small signaling molecules, called autoinducers (AIs), that are secreted and …
mediated by small signaling molecules, called autoinducers (AIs), that are secreted and …
Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr
DS Garrett, YJ Seok, A Peterkofsky… - nature structural …, 1999 - nature.com
The solution structure of the first protein–protein complex of the bacterial
phosphoenolpyruvate: sugar phosphotransferase system between the N–terminal domain of …
phosphoenolpyruvate: sugar phosphotransferase system between the N–terminal domain of …
Solution Structure of the 30 kDa N-Terminal Domain of Enzyme I of the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System by …
DS Garrett, YJ Seok, DI Liao, A Peterkofsky… - Biochemistry, 1997 - ACS Publications
The three-dimensional solution structure of the 259-residue 30 kDa N-terminal domain of
enzyme I (EIN) of the phosphoenolpyruvate: sugar phosphotransferase system of …
enzyme I (EIN) of the phosphoenolpyruvate: sugar phosphotransferase system of …
Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr
BE Jones, V Dossonnet, E Kuster, W Hillen… - Journal of Biological …, 1997 - ASBMB
Catabolite repression of a number of catabolic operons in bacilli is mediated by the
catabolite control protein CcpA, the phosphocarrier protein HPr from the …
catabolite control protein CcpA, the phosphocarrier protein HPr from the …