1fj2
From Proteopedia
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Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution
Overview
BACKGROUND: 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. RESULTS: We have solved, the crystal structure of the human putative Galpha-regulatory protein acyl, thioesterase (hAPT1) with a ... [(full description)]
About this Structure
1FJ2 is a [Single protein] structure of sequence from [Homo sapiens] with BR as [ligand]. Active as [Alkylglycerophosphoethanolamine phosphodiesterase], with EC number [3.1.4.39]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A., Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS, Structure. 2000 Nov 15;8(11):1137-46. PMID:11080636
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