Optimal Efficiency of ClpAP and ClpXP Chaperone-Proteases Is Achieved by Architectural Symmetry

Structure

Volumn 17, Issue 4, 2009, Pages 508-516

  Maglica, Željka ^a   Kolygo, Kristina ^a   Weber Ban, Eilika ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

PROTEINS

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ENDOPEPTIDASE CLP; ENDOPEPTIDASE CLPA; ENDOPEPTIDASE CLPX; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME ACTIVITY; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DEGRADATION;

ADENOSINE TRIPHOSPHATASES; BINDING SITES; CATALYSIS; ENDOPEPTIDASE CLP; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLUORESCENCE RESONANCE ENERGY TRANSFER; KINETICS; LIGHT; MOLECULAR CHAPERONES; PROTEIN BINDING; SCATTERING, RADIATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SUBSTRATE SPECIFICITY;

EID: 64049095981     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.02.014     Document Type: Article

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