Acetylcholinesterase with acetylcholine

ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA (see also AChE inhibitors and substrates)

Overview

Solution of the three-dimensional (3D) structure of Torpedo californica acetylcholinesterase (TcAChE) in 1991 (Sussman et al. & Silman (1991)) opened up new horizons in research on an enzyme that had already been the subject of intensive investigation. The unanticipated structure of this extremely rapid enzyme, in which the active site was found to be buried at the bottom of a , lined by (colored darkmagenta), led to a revision of the views then held concerning substrate traffic, recognition, and hydrolysis (Botti et al. Sussman & Silman (1999)). This led to a series of theoretical and experimental studies, which took advantage of recent advances in theoretical techniques for treatment of proteins, such as molecular dynamics and electrostatics and to site-directed mutagenesis, utilizing suitable expression systems. Acetylcholinesterase hydrolysizes the neurotransmitter acetylcholine , producing group. ACh directly binds (via its nucleophilic Oγ atom) within the . The residues are also important in the ligand recognition. After this binding acetylcholinesterase ACh.

About this Structure

2ACE is a Single protein structure of sequence from Torpedo californica with ACH as ligand. This structure superseeds the now removed PDB entry 1ACE. Active as Acetylcholinesterase, with EC number 3.1.1.7 Structure known Active Site: CAT. Full crystallographic information is available from OCA.

Additional Resources

For additional information, see: Alzheimer's Disease