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A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein.

A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein. Research Abstract Details 

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  • A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein. Abstract Text:

    hwan younHwan Youn,robert l kerbyRobert L Kerby,junseock kohJunseock Koh,gary p robertsGary P Roberts,

    The cAMP receptor protein (CRP) of Escherichia coli exists in an equilibrium between active and inactive forms, and the effector, cAMP, shifts that equilibrium to the active form, thereby allowing DNA binding. For this equilibrium shift, a C-helix repositioning around the C-helix residues Thr-127 and Ser-128 has been reported as a critical local event along with proper beta4/beta5 positioning. Here we show that another C-helix residue, Arg-123, has a unique role in cAMP-dependent CRP activation in two different ways. First, Arg-123 is important for proper cAMP affinity, although it is not critical for the conformational change with saturating amounts of cAMP. Second, Arg-123 is optimal for stabilizing the inactive conformation of CRP when cAMP is absent, thereby allowing a maximal range of regulation by cAMP. However, Arg-123 does not appear to be critical for a functional response to cAMP, as has been proposed previously (Berman, H. M., Ten Eyck, L. F., Goodsell, D. S., Haste, N. M., Korney, A., and Taylor, S. S. (2005) Proc. Natl. Acad. Sci. U. S. A. 102, 45-50). Based on mutagenic evidence, we also propose the basis for the stabilization of the inactive form to be through a salt interaction between Asp-68 and Arg-123.

    A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein. Publishing Authors By Initials

    h younH Youn,rl kerbyRL Kerby,j kohJ Koh,gp robertsGP Roberts,

    For similar proteins: transcription factors research abstracts see: proteins: transcription factors research

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    A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: The Journal of biological chemistry

    VOLUME: 282

    Page Numbers: 3632-9

    Journal Abbreviation: J. Biol. Chem.

    ISSN: 0021-9258

    DAY: 8

    MONTH: 12

    YEAR: 2006

    A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985121

    A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein. Keywords Mesh Terms:

    KEYWORDS: Transcription Factors

    MESH TERMS: physiology

    Chemical & Substance for Abstract: A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein. Information

    Substance Name: Arginine

    Registry Number: 74-79-3

    Grant and Affiliation Information for A C-helix residue, Arg-123, has important roles in both the active and inactive forms of the cAMP receptor protein.

    AFFILIATION: Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: GM53228

    ACRONYM: GM

    MEDLINETA: J Biol Chem

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    ACCESSION NUMBER:

    Number Hits: 0

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