Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA(Glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system

Guangshun Wang, John M. Louis, Melissa Sondej, Yeong Jae Seok, Alan Peterkofsky, G. Marius Clore

Research output: Contribution to journalArticle

105 Citations (Scopus)

Abstract

The solution structure of the second protein-protein complex of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system, that between histidine-containing phosphocarrier protein (HPr) and glucose-specific enzyme IIA(Glucose) (IIA(Glc)), has been determined by NMR spectroscopy, including the use of dipolar couplings to provide long-range orientational information and newly developed rigid body minimization and constrained/restrained simulated annealing methods. A protruding convex surface on HPr interacts with a complementary concave depression on IIA(Glc). Both binding surfaces comprise a central hydrophobic core region surrounded by a ring of polar and charged residues, positive for HPr and negative for IIA(Glc). Formation of the unphosphorylated complex, as well as the phosphorylated transition state, involves little or no change in the protein backbones, but there are conformational rearrangements of the interfacial side chains. Both HPr and IIA(Glc) recognize a variety of structurally diverse proteins. Comparisons with the structures of the enzyme I-HPr and IIA(Glc)-glycerol kinase complexes reveal how similar binding surfaces can be formed with underlying backbone scaffolds that are structurally dissimilar and highlight the role of redundancy and side chain conformational plasticity.

Original languageEnglish (US)
Pages (from-to)5635-5649
Number of pages15
JournalEMBO Journal
Volume19
Issue number21
StatePublished - Nov 1 2000

Fingerprint

Phosphoenolpyruvate Sugar Phosphotransferase System
Escherichia coli
Proteins
Glucose
Enzymes
Glycerol Kinase
phosphocarrier protein HPr
Escherichia coli Proteins
Simulated annealing
Scaffolds
Nuclear magnetic resonance spectroscopy
Plasticity
Redundancy

Keywords

  • E.coli PEP:sugar PTS
  • Glucose-specific enzyme IIA(Glucose)
  • Histidine-containing phosphocarrier protein
  • NMR

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA(Glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. / Wang, Guangshun; Louis, John M.; Sondej, Melissa; Seok, Yeong Jae; Peterkofsky, Alan; Clore, G. Marius.

In: EMBO Journal, Vol. 19, No. 21, 01.11.2000, p. 5635-5649.

Research output: Contribution to journalArticle

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abstract = "The solution structure of the second protein-protein complex of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system, that between histidine-containing phosphocarrier protein (HPr) and glucose-specific enzyme IIA(Glucose) (IIA(Glc)), has been determined by NMR spectroscopy, including the use of dipolar couplings to provide long-range orientational information and newly developed rigid body minimization and constrained/restrained simulated annealing methods. A protruding convex surface on HPr interacts with a complementary concave depression on IIA(Glc). Both binding surfaces comprise a central hydrophobic core region surrounded by a ring of polar and charged residues, positive for HPr and negative for IIA(Glc). Formation of the unphosphorylated complex, as well as the phosphorylated transition state, involves little or no change in the protein backbones, but there are conformational rearrangements of the interfacial side chains. Both HPr and IIA(Glc) recognize a variety of structurally diverse proteins. Comparisons with the structures of the enzyme I-HPr and IIA(Glc)-glycerol kinase complexes reveal how similar binding surfaces can be formed with underlying backbone scaffolds that are structurally dissimilar and highlight the role of redundancy and side chain conformational plasticity.",
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