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

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, incl...

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Bibliographic Details
Published in:The EMBO journal 2000-11, Vol.19 (21), p.5635-5649
Main Authors: Wang, G, Louis, J M, Sondej, M, Seok, Y J, Peterkofsky, A, Clore, G M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Binding Sites
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli Proteins
Glycerol Kinase - chemistry
Glycerol Kinase - genetics
Macromolecular Substances
Magnetic Resonance Spectroscopy
Models, Molecular
Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry
Phosphoenolpyruvate Sugar Phosphotransferase System - genetics
Protein Conformation
Signal Transduction
Solutions
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Summary: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.
ISSN:0261-4189
DOI:10.1093/emboj/19.21.5635