| Autor: | G M Clore, Alan Peterkofsky, Angela M. Gronenborn, Yeong-Jae Seok, D.S. Garrett |
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| Rok vydání: | 1999 |
| Předmět: |
Chemistry
Stereochemistry macromolecular substances Nuclear magnetic resonance spectroscopy PEP group translocation Biochemistry symbols.namesake Crystallography Protein structure Structural Biology Genetics symbols bacteria Directionality Transferase van der Waals force Phosphoenolpyruvate carboxykinase Peptide sequence |
| Zdroj: | Nature Structural Biology. 6:166-173 |
| ISSN: | 1072-8368 |
| Popis: | The solution structure of the first protein-protein complex of the bacterial phosphoenolpyruvate: sugar phosphotransferase system between the N-terminal domain of enzyme I (EIN) and the histidine-containing phosphocarrier protein HPr has been determined by NMR spectroscopy, including the use of residual dipolar couplings that provide long-range structural information. The complex between EIN and HPr is a classical example of surface complementarity, involving an essentially all helical interface, comprising helices 2, 2', 3 and 4 of the alpha-subdomain of EIN and helices 1 and 2 of HPr, that requires virtually no changes in conformation of the components relative to that in their respective free states. The specificity of the complex is dependent on the correct placement of both van der Waals and electrostatic contacts. The transition state can be formed with minimal changes in overall conformation, and is stabilized in favor of phosphorylated HPr, thereby accounting for the directionality of phosphoryl transfer. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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