Escherichia coli cyclic AMP receptor protein mutants provide evidence for ligand contacts important in activation
| Autor: | M Kantorow, K McKenney, J Moore, D Vanderzwaag |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
Molecular Structure Cyclic AMP Receptor Protein Mutant lac operon Hydrogen Bonding Biology Ligands Ligand (biochemistry) medicine.disease_cause Microbiology Receptors Cyclic AMP Amino acid Biochemistry chemistry Cyclic AMP Escherichia coli Mutagenesis Site-Directed medicine Cloning Molecular Binding site Receptor Molecular Biology Research Article |
| Zdroj: | Journal of Bacteriology. 174:8030-8035 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | The three-dimensional model of the Escherichia coli cyclic AMP (cAMP) receptor protein (CRP) shows that several amino acids are involved as chemical contacts for binding cAMP. We have constructed and characterized mutants at four of these positions, E72, R82, S83, and R123. The mutations were made in wild-type crp as well as a cAMP-independent crp, crp*. The activities of the mutant proteins were characterized in vivo for their ability to activate the lac operon. These results provide genetic evidence to support that E72 and R82 are essential and S83 and R123 are important in the activation of CRP by cAMP. |
| Databáze: | OpenAIRE |
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