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1pja
From Proteopedia
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| - | [[Image:1pja.png|left|200px]] | ||
| - | + | ==The crystal structure of palmitoyl protein thioesterase-2 reveals the basis for divergent substrate specificities of the two lysosomal thioesterases (PPT1 and PPT2)== | |
| - | + | <StructureSection load='1pja' size='340' side='right'caption='[[1pja]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1pja]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PJA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
| - | == | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pja OCA], [https://pdbe.org/1pja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pja RCSB], [https://www.ebi.ac.uk/pdbsum/1pja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pja ProSAT]</span></td></tr> |
| - | [[1pja]] is a 1 chain structure with sequence from [ | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PPT2_HUMAN PPT2_HUMAN] Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, is unable to remove palmitate from peptides or proteins.<ref>PMID:9341199</ref> <ref>PMID:10417332</ref> <ref>PMID:12855696</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pj/1pja_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pja ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Thioesterase|Thioesterase]] | + | *[[Thioesterase 3D structures|Thioesterase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Biehl | + | [[Category: Biehl ER]] |
| - | [[Category: Calero | + | [[Category: Calero G]] |
| - | [[Category: Clardy | + | [[Category: Clardy J]] |
| - | [[Category: Gupta | + | [[Category: Gupta P]] |
| - | [[Category: Hofmann | + | [[Category: Hofmann SL]] |
| - | [[Category: Nonato | + | [[Category: Nonato MC]] |
| - | [[Category: Tandel | + | [[Category: Tandel S]] |
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Current revision
The crystal structure of palmitoyl protein thioesterase-2 reveals the basis for divergent substrate specificities of the two lysosomal thioesterases (PPT1 and PPT2)
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Categories: Homo sapiens | Large Structures | Biehl ER | Calero G | Clardy J | Gupta P | Hofmann SL | Nonato MC | Tandel S
