1FJ2

Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution

Summary for 1FJ2

• Entry DOI: 10.2210/pdb1fj2/pdb
• Related: 1auo
• Descriptor: PROTEIN (ACYL PROTEIN THIOESTERASE 1), BROMIDE ION (3 entities in total)
• Functional Keywords: alpha/beta hydrolase, serine hydrolase, sad, anomalous diffraction, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : O75608
• Total number of polymer chains: 2
• Total formula weight: 53037.68

Authors

Devedjiev, Y.,Dauter, Z.,Kuznetsov, S.,Jones, T.,Derewenda, Z. (deposition date: 2000-08-07, release date: 2000-11-29, Last modification date: 2024-02-07)

Primary citation

Devedjiev, Y.,Dauter, Z.,Kuznetsov, S.R.,Jones, T.L.,Derewenda, Z.S.
Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A.
Structure Fold.Des., 8:1137-1146, 2000

PubMed Abstract: Many proteins undergo posttranslational modifications involving covalent attachment of lipid groups. Among them is palmitoylation, a dynamic, reversible process that affects trimeric G proteins and Ras and constitutes a regulatory mechanism for signal transduction pathways. Recently, an acylhydrolase previously identified as lysophospholipase has been shown to function as an acyl protein thioesterase, which catalyzes depalmitoylation of Galpha proteins as well as Ras. Its amino acid sequence suggested that the protein is evolutionarily related to neutral lipases and other thioesterases, but direct structural information was not available.

PubMed: 11080636
DOI: 10.1016/S0969-2126(00)00529-3

Experimental method

X-RAY DIFFRACTION (1.5 Å)