Trans-acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication

Journal of Biological Chemistry

Volumn 289, Issue 47, 2014, Pages 32965-32976

  Zeymer, Cathleen ^a   Fischer, Sebastian ^a   Reinstein, Jochen ^a  

^a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; HYDROLYSIS; NUCLEOTIDES; OLIGOMERIZATION; OLIGOMERS; PROTEINS;

ALLOSTERIC REGULATION; CELLULAR ACTIVITIES; CHAPERONE SYSTEMS; MECHANISTIC STUDIES; MOLECULAR CHAPERONES; NUCLEOTIDE BINDING; NUCLEOTIDE-BINDING DOMAIN; SUBUNIT INTERFACES;

ARGININE;

ADENOSINE TRIPHOSPHATE; ARGININE; ATPASES ASSOCIATED WITH VARIOUS CELLULAR ACTIVITIES PROTEIN; CHAPERONE; DIMER; NUCLEOTIDE; PROTEIN CLPB; PROTEIN VARIANT; REGULATOR PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; HEAT SHOCK PROTEIN; PROTEIN BINDING;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; BIOENGINEERING; CONTROLLED STUDY; COVALENT BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SPECIFICITY; OLIGOMERIZATION; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN HYDROLYSIS; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HYDROLYSIS; KINETICS; METABOLISM; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; THERMUS THERMOPHILUS;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ALLOSTERIC REGULATION; ARGININE; BACTERIAL PROTEINS; BINDING SITES; HEAT-SHOCK PROTEINS; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MUTATION; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; THERMUS THERMOPHILUS;

EID: 84911450146     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.608828     Document Type: Article

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