Your cellular trash cans go through a series
of checks before compacting the trash.
"The 26S proteasome is a 2.5 MDa molecular machine that executes
Our analysis reveals the existence of three major conformations: in addition to the previously described ATP-hydrolyzing (ATPh) and ATP-γS conformations, an intermediate state has been found.
the degradation of substrates of the ubiquitin–proteasome pathway. The molecular architecture of the 26S proteasome was recently established by cryo-EM approaches.
Our analysis reveals the existence of three major conformations: in addition to the previously described ATP-hydrolyzing (ATPh) and ATP-γS conformations, an intermediate state has been found.
Its AAA-ATPase module adopts essentially the same topology that is observed in the ATPh conformation, whereas the lid is more similar to the ATP-γS bound state.
Based on the conformational ensemble of the 26S proteasome in solution, we propose a mechanistic model for substrate recognition, commitment, deubiquitylation, and translocation into the core particle."
PNAS
Complexity = DESIGN, hence a DESIGNER
I will praise thee;
for I am fearfully and wonderfully made:
marvellous are thy works;
Psalm 139:14
