1eh5
From Proteopedia
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CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1 COMPLEXED WITH PALMITATE
Overview
Mutations in palmitoyl-protein thioesterase 1 (PPT1), a lysosomal enzyme, that removes fatty acyl groups from cysteine residues in modified, proteins, cause the fatal inherited neurodegenerative disorder infantile, neuronal ceroid lipofuscinosis. The accumulation of undigested substrates, leads to the formation of neuronal storage bodies that are associated with, the clinical symptoms. Less severe forms of PPT1 deficiency have been, found recently that are caused by a distinct set of PPT1 mutations, some, of which retain a small amount of thioesterase activity. We have, determined the crystal structure of PPT1 with and without bound palmitate, by using multiwavelength anomalous diffraction phasing. The structure, reveals an alpha/beta-hydrolase fold with a catalytic triad composed of, Ser115-His289-Asp233 and provides insights into the structural basis for, the phenotypes associated with PPT1 mutations.
About this Structure
1EH5 is a Single protein structure of sequence from Bos taurus with NDG and PLM as ligands. Active as Palmitoyl-protein hydrolase, with EC number 3.1.2.22 Full crystallographic information is available from OCA.
Reference
The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis., Bellizzi JJ 3rd, Widom J, Kemp C, Lu JY, Das AK, Hofmann SL, Clardy J, Proc Natl Acad Sci U S A. 2000 Apr 25;97(9):4573-8. PMID:10781062
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