Mutations that alter the allosteric nature of cAMP receptor protein of Escherichia coli.
about
The structure of a CAP-DNA complex having two cAMP molecules bound to each monomerCharacterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a cyclic AMP receptor protein-like DNA binding protein.Two-state allosteric modeling suggests protein equilibrium as an integral component for cyclic AMP (cAMP) specificity in the cAMP receptor protein of Escherichia coli.Cooperative DNA binding of heterologous proteins: evidence for contact between the cyclic AMP receptor protein and RNA polymeraseCatabolite gene activator protein mutations affecting activity of the araBAD promoter.Experimental evolution reveals an effective avenue to release catabolite repression via mutations in XylR.Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli.Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: targeting positions 72 and 82 of the cyclic nucleotide binding pocketCyclic AMP in prokaryotes.Characterization of the binding of cAMP and cGMP to the CRP*598 mutant of the E. coli cAMP receptor proteinRoles of catabolite activator protein sites centered at -81.5 and -41.5 in the activation of the Klebsiella aerogenes histidine utilization operon hutUH.Pivotal role of amino acid at position 138 in the allosteric hinge reorientation of cAMP receptor protein.Effect of Salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and pH-regulated protein synthesis.Fnr mutants that activate gene expression in the presence of oxygenEscherichia coli catabolite gene activator protein mutants defective in positive control of lac operon transcription.Genetic analysis of transcriptional activation and repression in the Tn21 mer operonCyclic AMP-induced conformational change of cyclic AMP receptor protein (CRP): intragenic suppressors of cyclic AMP-independent CRP mutationsStudy of highly constitutively active mutants suggests how cAMP activates cAMP receptor protein.Cyclic AMP signalling in mycobacteria: redirecting the conversation with a common currencyAllosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.Single amino acid substitutions in the cAMP receptor protein specifically abolish regulation by the CytR repressor in Escherichia coli.A Xanthomonas campestris pv. campestris protein similar to catabolite activation factor is involved in regulation of phytopathogenicity.Nucleotide sequence and characterization of the sfs1 gene: sfs1 is involved in CRP*-dependent mal gene expression in Escherichia coli.Mutations in the cyclic AMP binding site of the cyclic AMP receptor protein of Escherichia coli.Catabolic regulation analysis of Escherichia coli and its crp, mlc, mgsA, pgi and ptsG mutantsTranscriptional effects of CRP* expression in Escherichia coli.Cloning and sequencing of an Escherichia coli gene, nlp, highly homologous to the ner genes of bacteriophages Mu and D108.Cloning of the fic-1 gene involved in cell filamentation induced by cyclic AMP and construction of a delta fic Escherichia coli strain.Mutations that alter the ability of the Escherichia coli cyclic AMP receptor protein to activate transcription.Cyclic AMP-dependent osmoregulation of crp gene expression in Escherichia coli.Quantifying Allosteric Communication via Both Concerted Structural Changes and Conformational Disorder with CARDS.
P2860
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P2860
Mutations that alter the allosteric nature of cAMP receptor protein of Escherichia coli.
description
1985 nî lūn-bûn
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1985年の論文
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1985年論文
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1985年論文
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1985年論文
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1985年論文
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1985年論文
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1985年论文
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1985年论文
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1985年论文
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name
Mutations that alter the allosteric nature of cAMP receptor protein of Escherichia coli.
@en
type
label
Mutations that alter the allosteric nature of cAMP receptor protein of Escherichia coli.
@en
prefLabel
Mutations that alter the allosteric nature of cAMP receptor protein of Escherichia coli.
@en
P2093
P2860
P1433
P1476
Mutations that alter the allosteric nature of cAMP receptor protein of Escherichia coli.
@en
P2093
P2860
P304
P407
P577
1985-12-01T00:00:00Z