Substrate-translocating loops regulate mechanochemical coupling and power production in AAA+ protease ClpXP

Nature Structural and Molecular Biology

Volumn 23, Issue 11, 2016, Pages 974-981

  Rodriguez Aliaga, Piere ^a,b   Ramirez, Luis ^a,b   Kim, Frank ^a   Bustamante, Carlos ^a,b   Martin, Andreas ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; CLPXP PROTEIN; PROTEINASE; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; CLPX PROTEIN, E COLI; CLPXP PROTEASE, E COLI; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEIN; PROTEIN BINDING;

ARTICLE; BULK DENSITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME RELEASE; ENZYME SUBSTRATE; ESCHERICHIA COLI; GRIP STRENGTH; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN HOMEOSTASIS; PROTEIN HYDROLYSIS; PROTEIN PROCESSING; PROTEIN UNFOLDING; REGULATORY MECHANISM; CHEMISTRY; ENZYME SPECIFICITY; HYDROLYSIS; KINETICS; METABOLISM; MOLECULAR MODEL; PROTEIN CONFORMATION;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ENDOPEPTIDASE CLP; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN UNFOLDING; SUBSTRATE SPECIFICITY;

EID: 84988689906     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3298     Document Type: Article

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