Related Experiment Video
Updated: Jul 15, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Structural characterization of dimeric murine aminoacylase III
Sergey Ryazantsev1, Natalia Abuladze, Debra Newman
1Department of Biological Chemistry, David Geffen School of Medicine, University of California at Los Angeles, Room 33-080 CHS, 10833 Le Conte Avenue, CA 90095-1689, USA.
Abstract:
Aminoacylase III (AAIII) plays an important role in deacetylation of acetylated amino acids and N-acetylated S-cysteine conjugates of halogenated alkenes and alkanes. AAIII, recently cloned from mouse kidney and partially characterized, is a mixture of tetramers and dimers. In the present work, AAIII dimers were purified and shown to be enzymatically active. Limited trypsinolysis showed two domains of approximately 9 and 25 kDa. The three-dimensional structure of the dimer was studied by electron microscopy of negative stained samples and by single-particle reconstruction. A 16A resolution model of the AAIII dimer was created. It has an unusual, cage-like, structure. A realistic AAIII tetramer model was built from two dimers.
Related Concept Videos
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Protein Folding
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence.
Overview of Myosin Structure and Function
Structure of Amines

