Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
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Prokaryotic genome regulation: a revolutionary paradigmThe structure of the T127L/S128A mutant of cAMP receptor protein facilitates promoter site bindingStructural basis for cAMP-mediated allosteric control of the catabolite activator protein.Mapping Conformational Transitions in Cyclic AMP Receptor Protein: Crystal Structure and Normal-Mode Analysis of Mycobacterium tuberculosis apo-cAMP Receptor ProteinKinetic studies of cAMP-induced allosteric changes in cyclic AMP receptor protein from Escherichia coliTwo-state allosteric modeling suggests protein equilibrium as an integral component for cyclic AMP (cAMP) specificity in the cAMP receptor protein of Escherichia coli.Novel roles of cAMP receptor protein (CRP) in regulation of transport and metabolism of carbon sources.Sequence variations within PrfA DNA binding sites and effects on Listeria monocytogenes virulence gene expression.Intracellular induction of Listeria monocytogenes actA expressionDynamic fluctuations provide the basis of a conformational switch mechanism in apo cyclic AMP receptor protein.Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: targeting positions 72 and 82 of the cyclic nucleotide binding pocketDownregulation of the Escherichia coli guaB promoter by upstream-bound cyclic AMP receptor protein.Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: targeting positions 83, 127 and 128 of the cyclic nucleotide binding pocketPivotal role of amino acid at position 138 in the allosteric hinge reorientation of cAMP receptor protein.Mapping cyclic nucleotide-induced conformational changes in cyclicAMP receptor protein by a protein footprinting technique using different chemical proteases.Study of highly constitutively active mutants suggests how cAMP activates cAMP receptor protein.The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein.DNA-binding properties of a cGMP-binding CRP homologue that controls development of metabolically dormant cysts of Rhodospirillum centenum.Functional impact of mutational activation on the Listeria monocytogenes central virulence regulator PrfA.Profound asymmetry in the structure of the cAMP-free cAMP Receptor Protein (CRP) from Mycobacterium tuberculosisCrystallization and preliminary X-ray diffraction analysis of D53H mutant Escherichia coli cAMP receptor protein.Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP.Transcription activation at the Escherichia coli melAB promoter: the role of MelR and the cyclic AMP receptor protein.Functional similarities between the Listeria monocytogenes virulence regulator PrfA and cyclic AMP receptor protein: the PrfA* (Gly145Ser) mutation increases binding affinity for target DNA.A Gly145Ser substitution in the transcriptional activator PrfA causes constitutive overexpression of virulence factors in Listeria monocytogenes.Guanidine hydrochloride-induced unfolding of the three heme coordination states of the CO-sensing transcription factor, CooA.The Escherichia coli RNA polymerase alpha subunit linker: length requirements for transcription activation at CRP-dependent promoters.Growth on glucose decreases cAMP-CRP activity while paradoxically increasing intracellular cAMP in the light-organ symbiont Vibrio fischeri.Global regulators orchestrate group II intron retromobility.Opposite allosteric mechanisms in TetR and CAP.Adaptation in bacterial flagellar and motility systems: from regulon members to 'foraging'-like behavior in E. coli.Interactive and dominant effects of residues 128 and 141 on cyclic nucleotide and DNA bindings in Escherichia coli cAMP receptor protein.Contributions of [4Fe-4S]-FNR and integration host factor to fnr transcriptional regulation.Residue threonine-149 of the Salmonella typhimurium CysB transcription activator: mutations causing constitutive expression of positively regulated genes of the cysteine regulon.Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: lessons from a subunit-crosslinked form of CRP.
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P2860
Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on October 1992
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
@en
Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
@nl
type
label
Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
@en
Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
@nl
prefLabel
Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
@en
Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
@nl
P2093
P2860
P356
P1476
Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
@en
P2093
P2860
P304
P356
10.1073/PNAS.89.20.9700
P407
P577
1992-10-01T00:00:00Z