1EI9

CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1

Summary for 1EI9

• Entry DOI: 10.2210/pdb1ei9/pdb
• Related: 1EH5
• Descriptor: PALMITOYL PROTEIN THIOESTERASE 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: alpha/beta hydrolase, glycoprotein, hydrolase
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 32313.93

Authors

Bellizzi III, J.J.,Widom, J.,Kemp, C.,Lu, J.Y.,Das, A.K.,Hofmann, S.L.,Clardy, J. (deposition date: 2000-02-24, release date: 2000-04-26, Last modification date: 2024-11-20)

Primary citation

Bellizzi III, J.J.,Widom, J.,Kemp, C.,Lu, J.Y.,Das, A.K.,Hofmann, S.L.,Clardy, J.
The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis.
Proc.Natl.Acad.Sci.USA, 97:4573-4578, 2000

PubMed Abstract: 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.

PubMed: 10781062
DOI: 10.1073/pnas.080508097

Experimental method

X-RAY DIFFRACTION (2.25 Å)