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Article

Study of highly constitutively active mutants suggests how cAMP activates cAMP receptor protein.

The Journal of biological chemistry - 13 Jan 2006

Youn Hwan, Kerby Robert L, Conrad Mary, Roberts Gary P

Abstract excerpt

The cAMP receptor protein (CRP) of Escherichia coli undergoes a conformational change in response to cAMP binding that allows it to bind specific DNA sequences. Using an in vivo screening method following the simultaneous randomization of the codons at positions 127 and 128 (two C-helix residues of the protein interacting with cAMP), we have isolated a series of novel constitutively active CRP variants. Sequence...

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Identifiers

PMID: 16260780
DOI: 10.1074/jbc.M509421200
PMCID: PMC3464001

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CRP

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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Study of highly constitutively active mutants suggests how cAMP activates cAMP receptor protein.PMID 16260780Read ↗

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

The structure of the T127L/S128A mutant of cAMP receptor protein facilitates promoter site binding.Semantic proximity Read ↗

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

The effect of Ser 128 substitution on the structure and stability of cAMP receptor protein from Escherichia coli.Semantic proximity Read ↗

A mutant spacer sequence between -35 and -10 elements makes the Plac promoter hyperactive and cAMP receptor protein-independent.Semantic proximity Read ↗

Mutations that alter the ability of the Escherichia coli cyclic AMP receptor protein to activate transcription.Semantic proximity Read ↗

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 ↗

The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein.Semantic proximity Read ↗

Dissection of a surface-exposed portion of the cAMP-CRP complex that mediates transcription activation and repression.Semantic proximity Read ↗

Intersubunit association induces unique allosteric dependence of the T127L CRP mutant on pH.Semantic proximity Read ↗

Crystallization and preliminary X-ray diffraction analysis of D53H mutant Escherichia coli cAMP receptor protein.Semantic proximity Read ↗

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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