| Literature DB >> 19732826 |
Wolfgang Kress1, Zeljka Maglica, Eilika Weber-Ban.
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.Entities:
Mesh:
Substances:
Year: 2009 PMID: 19732826 DOI: 10.1016/j.resmic.2009.08.006
Source DB: PubMed Journal: Res Microbiol ISSN: 0923-2508 Impact factor: 3.992