1ei9: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1== | ==CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1== | ||
<StructureSection load='1ei9' size='340' side='right' caption='[[1ei9]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='1ei9' size='340' side='right'caption='[[1ei9]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ei9]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ei9]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI9 FirstGlance]. <br> | ||
| Line 30: | Line 30: | ||
</div> | </div> | ||
<div class="pdbe-citations 1ei9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1ei9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Thioesterase|Thioesterase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 35: | Line 38: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bovin]] | [[Category: Bovin]] | ||
[[Category: Large Structures]] | |||
[[Category: Palmitoyl-protein hydrolase]] | [[Category: Palmitoyl-protein hydrolase]] | ||
[[Category: Clardy, J]] | [[Category: Clardy, J]] | ||
Revision as of 12:14, 6 November 2019
CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1CRYSTAL STRUCTURE OF PALMITOYL PROTEIN THIOESTERASE 1
Structural highlights
Function[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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMutations 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||