The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function.

The Journal of biological chemistry

Volumn 278, Issue 49, 2003, Pages 48981-48990

  Wojtyra, Urszula A ^a   Thibault, Guillaume ^a   Tuite, Ashleigh ^a   Houry, Walid A ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; CLPX PROTEIN, E COLI; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEIN; ZINC;

ANIMAL; ARTICLE; BINDING SITE; CHEMISTRY; CIRCULAR DICHROISM; DIMERIZATION; ENZYME LINKED IMMUNOSORBENT ASSAY; GENETICS; METABOLISM; MUTAGENESIS; PHYSIOLOGY;

ADENOSINE TRIPHOSPHATASES; ANIMALS; BINDING SITES; CIRCULAR DICHROISM; DIMERIZATION; ENDOPEPTIDASE CLP; ENZYME-LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI PROTEINS; MOLECULAR CHAPERONES; MUTAGENESIS; ZINC;

EID: 1242289869     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M307825200     Document Type: Article

References (0)