Ontology highlight
ABSTRACT:
SUBMITTER: Andersson FI
PROVIDER: S-EPMC2679453 | biostudies-literature | 2009 May
REPOSITORIES: biostudies-literature
Andersson Fredrik I FI Tryggvesson Anders A Sharon Michal M Diemand Alexander V AV Classen Mirjam M Best Christoph C Schmidt Ronny R Schelin Jenny J Stanne Tara M TM Bukau Bernd B Robinson Carol V CV Witt Susanne S Mogk Axel A Clarke Adrian K AK
The Journal of biological chemistry 20090223 20
The Clp protease is conserved among eubacteria and most eukaryotes, and uses ATP to drive protein substrate unfolding and translocation into a chamber of sequestered proteolytic active sites. The main constitutive Clp protease in photosynthetic organisms has evolved into a functionally essential and structurally intricate enzyme. The model Clp protease from the cyanobacterium Synechococcus consists of the HSP100 molecular chaperone ClpC and a mixed proteolytic core comprised of two distinct subu ...[more]