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Proteins: Structure, Function, and Engineering pp 303–321Cite as

Role of Allosteric Changes in Cyclic AMP Receptor Protein Function

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Part of the book series: Subcellular Biochemistry ((SCBI,volume 24))

Abstract

The idea that conformational changes may be controlled by a ligand binding was first pointed out in explaining the hornotropic cooperative binding of O2 to hemoglobin which has four O2 binding sites (Wyman, 1948; Wyman and Allen, 1951). The term reversible allosteric transition, which is an expression of such ligand-induced conformational changes, was introduced later (Monod and Jacob, 1961; Monod et al., 1963). An ideal system to study allostery is the interaction of cyclic AMP (cAMP) and its receptor protein (CRP). cAMP and CRP are two “master elements” of a vast global regulatory network in Escherichia coli (reviewed in Kolb et al., 1993). The level of cAMP dramatically changes in response to the nature of energy sources for cell growth. The CRP level also varies in the cell depending on the energy sources. When present in effective concentrations, cAMP binds to CRP, and the resulting complex regulates transcription of many genes. The most studied role of the cAMP-CRP complex is its role as an activator of transcription initiation. The protein is a homodimer of a 209 amino acid subunit. Two molecules of cAMP can bind to CRP, one to each subunit.

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Authors and Affiliations

  1. Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, 20892, USA

    Sankar Adhya, Sangryeol Ryu & Susan Garges

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  1. Sankar Adhya
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  2. Sangryeol Ryu
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  3. Susan Garges
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Editors and Affiliations

  1. Department of Biophysics, Bose Institute, Calcutta, 700054, India

    B. B. Biswas  & Siddhartha Roy  & 

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Adhya, S., Ryu, S., Garges, S. (1995). Role of Allosteric Changes in Cyclic AMP Receptor Protein Function. In: Biswas, B.B., Roy, S. (eds) Proteins: Structure, Function, and Engineering. Subcellular Biochemistry, vol 24. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1727-0_10

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  • DOI: https://doi.org/10.1007/978-1-4899-1727-0_10

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