Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
| Autor: | Vladimir N. Uversky, V. V. Rogov, Konstantin S. Vassilenko, Victor P. Kutyshenko, Protasova NYu, A. T. Gudkov |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Protein Denaturation
Circular dichroism Magnetic Resonance Spectroscopy Stereochemistry Calorimetry Ligands Biochemistry Protein Structure Secondary Mice Structure-Activity Relationship Protein structure Dihydrofolate reductase Escherichia coli Animals Urea Molecular Biology biology Chemistry Circular Dichroism Chaperonin 60 Circular permutation in proteins Molten globule Protein tertiary structure Protein Structure Tertiary Folding (chemistry) Tetrahydrofolate Dehydrogenase Crystallography Mutagenesis biology.protein Protein folding Research Article |
| Zdroj: | Protein Science. 5:1844-1851 |
| ISSN: | 1469-896X 0961-8368 |
| DOI: | 10.1002/pro.5560050910 |
| Popis: | It is obvious that functional activity of a protein molecule is closely related to its structure. On the other hand, the understanding of structure-function relationship still remains one of the intriguing problems of molecular biology. There is widespread belief that mutagenesis presents a real way to solve this problem. Following this assumption, we have investigated the effect of circular permutation in dihydrofolate reductase from E. coli on protein structure and functioning. It has been shown that in the absence of ligands two circularly permuted variants of dihydrofolate reductase possess all the properties of the molten globule state. However, after addition of ligands they gain the native-like structural properties and specific activity. This means that the in vitro folding of permuted dihydrofolate reductase is terminated at the stage of the molten globule formation. Interaction of permuted protein with ligands leads to the structural adjustment and formation of active protein molecules. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text