3.4.21.B50	dodecamer	12 * 48000-50000, dynamic light-scattering, DegQ assembles into large, cage-like dodecamers that form independently of unfolded substrate proteins. Dodecamer-formation is essential for the degradation of substrate proteins but not for the chaperone activity of DegQ	718323	
3.4.21.B50	dodecamer	12 * 50000, SDS-PAGE	651624	
3.4.21.B50	dodecamer	substrate-containing form, 12 * 50000, SDS-PAGE	718408	
3.4.21.B50	hexamer	6 * 50000, SDS-PAGE	651624	
3.4.21.B50	additional information	DegQLp forms predominantly trimers in the substrate-free state. In vitro, oligomerization is influenced by the pH of the protein solution and the presence of co-purified peptides binding to the PDZ1 and/or protease site. Misfolded proteins or peptides promote the assembly of protease active 12- or 24-mers the assembly of proteolytically active	-, 754420	
3.4.21.B50	trimer	substrate-free form	718408