1ei9

<table><tr><td colspan='2'>[[1ei9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EI9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eh5|1eh5]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Palmitoyl-protein_hydrolase Palmitoyl-protein hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.22 3.1.2.22] </span></td></tr>

[[https://www.uniprot.org/uniprot/PPT1_BOVIN PPT1_BOVIN]] Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10781062</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ei9" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bovin]]

[[Category: Palmitoyl-protein hydrolase]]

[[Category: Clardy, J]]

[[Category: Das, A K]]

[[Category: Hofmann, S L]]

[[Category: III, J J.Bellizzi]]

[[Category: Kemp, C]]

[[Category: Lu, J Y]]

[[Category: Widom, J]]

[[Category: Hydrolase]]