Related Experiment Video
Updated: Apr 30, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
J Wang1, J A Hartling, J M Flanagan
1Biology Department, Brookhaven National Laboratory, Upton, New York 11973-5000, USA.
Abstract:
We have determined the crystal structure of the proteolytic component of the caseinolytic Clp protease (ClpP) from E. coli at 2.3 A resolution using an ab initio phasing procedure that exploits the internal 14-fold symmetry of the oligomer. The structure of a ClpP monomer has a distinct fold that defines a fifth structural family of serine proteases but a conserved catalytic apparatus. The active protease resembles a hollow, solid-walled cylinder composed of two 7-fold symmetric rings stacked back-to-back. Its 14 proteolytic active sites are located within a central, roughly spherical chamber approximately 51 A in diameter. Access to the proteolytic chamber is controlled by two axial pores, each having a minimum diameter of approximately 10 A. From the structural features of ClpP, we suggest a model for its action in degrading proteins.
Related Concept Videos
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Ligand Binding and Linkage
ATP Synthase: Mechanism
ATP Synthase: Structure
The ADP/ATP Carrier Protein
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...

