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Article

Kinetic studies of cAMP-induced allosteric changes in mutants T127I, S128A, and T127I/S128A of the cAMP receptor protein from Escherichia coli.

The Journal of biological chemistry - 31 Oct 2003

Polit Agnieszka, Bonarek Piotr, Kepys Barbara, Kedracka-Krok Sylwia, Górecki Andrzej, Wasylewski Zygmunt

Abstract excerpt

The cAMP receptor protein (CRP) regulates the expression of several genes in Escherichia coli. The protein is a homodimer, and each monomer is folded into two distinct structural domains. After allosteric transitions resulting from the binding of cAMP, CRP specifically binds to DNA and activates...

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PMID: 12939272
DOI: 10.1074/jbc.M306398200

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CRP

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-12939272-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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Kinetic studies of cAMP-induced allosteric changes in mutants T127I, S128A, and T127I/S128A of the cAMP receptor protein from Escherichia coli.PMID 12939272Read ↗

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Allosteric regulation of the cAMP receptor protein.Semantic proximity Read ↗

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Characterization of the binding of cAMP and cGMP to the CRP*598 mutant of the E. coli cAMP receptor protein.Semantic proximity Read ↗

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Position 127 amino acid substitutions affect the formation of CRP:cAMP:lacP complexes but not CRP:cAMP:RNA polymerase complexes at lacP.Semantic proximity Read ↗

Determination of the conformations of cAMP receptor protein and its T127L,S128A mutant with and without cAMP from small angle neutron scattering measurements.Semantic proximity Read ↗

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