Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP

Escherichia coli ClpX, a member of the Clp family of ATPases, has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpP. Gel filtration and electron microscopy showed that ClpX subunits (Mr 46, 000) associate to form a six-membered ring...

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Veröffentlicht in:	The Journal of biological chemistry 1998-05, Vol.273 (20), p.12476-12481
Hauptverfasser:	Grimaud, R, Kessel, M, Beuron, F, Steven, A C, Maurizi, M R
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - isolation & purification Adenosine Triphosphatases - metabolism ATPases Associated with Diverse Cellular Activities Bacteriology Biochemistry, Molecular Biology Chromatography, Gel Endopeptidase Clp Escherichia coli - enzymology Escherichia coli Proteins Hydrolysis Life Sciences Microbiology and Parasitology Microscopy, Electron Molecular Chaperones - chemistry Molecular Chaperones - metabolism Protein Conformation Serine Endopeptidases - chemistry Serine Endopeptidases - isolation & purification Serine Endopeptidases - metabolism Structural Biology Substrate Specificity
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