1MT5

CRYSTAL STRUCTURE OF FATTY ACID AMIDE HYDROLASE

Summary for 1MT5

• Entry DOI: 10.2210/pdb1mt5/pdb
• Descriptor: Fatty-acid amide hydrolase, METHYL ARACHIDONYL FLUOROPHOSPHONATE (2 entities in total)
• Functional Keywords: amidase signature, hydrolase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Endoplasmic reticulum membrane; Single-pass membrane protein: P97612
• Total number of polymer chains: 16
• Total formula weight: 949016.21

Authors

Bracey, M.H.,Hanson, M.A.,Masuda, K.R.,Stevens, R.C.,Cravatt, B.F. (deposition date: 2002-09-20, release date: 2002-12-18, Last modification date: 2024-10-16)

Primary citation

Bracey, M.H.,Hanson, M.A.,Masuda, K.R.,Stevens, R.C.,Cravatt, B.F.
Structural Adaptations in a Membrane Enzyme That Terminates Endocannabinoid Signaling
science, 298:1793-1796, 2002

PubMed Abstract: Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.

PubMed: 12459591
DOI: 10.1126/science.1076535

Experimental method

X-RAY DIFFRACTION (2.8 Å)