Article
Allosteric regulation of the cAMP receptor protein.
Biochimica et biophysica acta - 5 May 2001
Harman J G
Abstract excerpt
The cyclic AMP receptor protein (CRP) of Escherichia coli is a dimer made up of identical subunits. Each CRP subunit contains a cyclic nucleotide binding pocket and the CRP dimer exhibits negative cooperativity in binding cAMP. In solutions containing cAMP, CRP undergoes sequential conformation changes from the inactive apo-form through the active CRP:(cAMP)(1) complex to the less active CRP:(cAMP)(2) complex...
Topics
- Allosteric Regulation
- Binding Sites
- Cyclic AMP
- DNA-Directed RNA Polymerases
- Escherichia coli
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Mutation
- Protein Conformation
- Receptors, Cyclic AMP