title: Clp chaperone-proteases: structure and function.
abstract: Clp proteases are the most widespread energy-dependent proteases in bacteria. Their two-component architecture of protease core and ATPase rings results in an inventory of several Clp protease complexes that often coexist. Here, we present insights into Clp protease function, from their assembly to substrate recruitment and processing, and how this is coupled to the expense of energy.
authors.affiliation: ETH Zurich, Institute of Molecular Biology & Biophysics, Schafmattstrasse 20, 8093 Zurich, Switzerland.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Kress
authors.forename: Zeljka
authors.initials: Z
authors.lastname: Maglica
authors.forename: Eilika
authors.initials: E
authors.lastname: Weber-Ban
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D049071:Endopeptidase Clp / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D018832:Molecular Chaperones; D049071:Endopeptidase Clp