Electrostatic occlusion and quaternary structural ion pairing are key determinants of Cu(I)-mediated allostery in the copper-sensing operon repressor (CsoR)

Biochemistry

Volumn 54, Issue 15, 2015, Pages 2463-2472

  Chang, Feng Ming James ^a   Martin, Julia E ^a   Giedroc, David P ^a  

^a INDIANA UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOINFORMATICS; COMPLEXATION; COPPER; DNA; DYES; ELECTROSTATICS; ENZYME ACTIVITY; GENE EXPRESSION; IONS; OLIGOMERS;

ALLOSTERIC REGULATION; BIOINFORMATICS ANALYSIS; CHARGED RESIDUES; COPPER RESISTANCE GENES; DNA BINDING ACTIVITY; GEOBACILLUS THERMODENITRIFICANS; KEY DETERMINANTS; SEQUENCE SIMILARITY;

COPPER COMPOUNDS;

BACTERIAL DNA; CUPROUS ION; HYDROGEN; TETRAMER; BACTERIAL PROTEIN; COPPER; PROTEIN BINDING; REPRESSOR PROTEIN;

ALLOSTERISM; ANISOTROPY; ARTICLE; BASE PAIRING; BINDING AFFINITY; BINDING SITE; CLADISTICS; CONTROLLED STUDY; COPPER SENSING OPERON REPRESSOR; CRYSTAL STRUCTURE; DNA BINDING; DNA PROTEIN COMPLEX; GEOBACILLUS; GEOBACILLUS THERMODENITRIFICANS; HYDROGEN BOND; ISOTHERMAL TITRATION CALORIMETRY; LISTERIA MONOCYTOGENES; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; QUANTITATIVE ANALYSIS; REPRESSOR GENE; STATIC ELECTRICITY; STOICHIOMETRY; SUBSTITUTION REACTION; TEMPERATURE DEPENDENCE; WILD TYPE; AMINO ACID SUBSTITUTION; CHEMISTRY; GENETICS; METABOLISM; MISSENSE MUTATION; MUTAGENESIS; PHYSIOLOGY; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE;

GEOBACILLUS THERMODENITRIFICANS;

ALLOSTERIC REGULATION; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; COPPER; DNA, BACTERIAL; GEOBACILLUS; MUTAGENESIS; MUTATION, MISSENSE; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; STATIC ELECTRICITY;

EID: 84928566001     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00154     Document Type: Article

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