At Sixes and Sevens: Characterization of the Symmetry Mismatch of the ClpAP Chaperone-Assisted Protease

ClpAP, a typical energy-dependent protease, consists of a proteolytic component (ClpP) and a chaperone-like ATPase (ClpA). ClpP is composed of two apposed heptameric rings, whereas in the presence of ATP or ATPγS, ClpA is a single hexameric ring. Formation of ClpAP complexes involves a symmetry mism...

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Veröffentlicht in:	Journal of structural biology 1998-11, Vol.123 (3), p.248-259
Hauptverfasser:	Beuron, Fabienne, Maurizi, Michael R., Belnap, David M., Kocsis, Eva, Booy, Frank P., Kessel, Martin, Steven, Alasdair C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - ultrastructure Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Bacterial Proteins - ultrastructure Clp protease Cryoelectron Microscopy electron microscopy Endopeptidase Clp energy-dependent proteolysis Escherichia coli - enzymology Escherichia coli Proteins Image Processing, Computer-Assisted Models, Molecular Protein Conformation Serine Endopeptidases - ultrastructure symmetry three-dimensional image reconstruction
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