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6ny9
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6ny9 is ON HOLD Authors: Cao, Y., Rice, P.A., Dickinson, B.C. Description: Alpha/beta hydrolase domain-containing protein 10 from mouse [[Category:...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Alpha/beta hydrolase domain-containing protein 10 from mouse== | |
| + | <StructureSection load='6ny9' size='340' side='right'caption='[[6ny9]], [[Resolution|resolution]] 1.66Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ny9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NY9 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]] 1.66Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</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=6ny9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ny9 OCA], [https://pdbe.org/6ny9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ny9 RCSB], [https://www.ebi.ac.uk/pdbsum/6ny9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ny9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ABHDA_MOUSE ABHDA_MOUSE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | S-Palmitoylation is a reversible lipid post-translational modification that has been observed on mitochondrial proteins, but both the regulation and functional consequences of mitochondrial S-palmitoylation are poorly understood. Here, we show that perturbing the 'erasers' of S-palmitoylation, acyl protein thioesterases (APTs), with either pan-active inhibitors or a mitochondrial-targeted APT inhibitor, diminishes the antioxidant buffering capacity of mitochondria. Surprisingly, this effect was not mediated by the only known mitochondrial APT, but rather by a resident mitochondrial protein with no known endogenous function, ABHD10. We show that ABHD10 is a member of the APT family of regulatory proteins and identify peroxiredoxin-5 (PRDX5), a key antioxidant protein, as a target of ABHD10 S-depalmitoylase activity. We then find that ABHD10 regulates the S-palmitoylation status of the nucleophilic active site residue of PRDX5, providing a direct mechanistic connection between ABHD10-mediated S-depalmitoylation of PRDX5 and its antioxidant capacity. | ||
| - | + | ABHD10 is an S-depalmitoylase affecting redox homeostasis through peroxiredoxin-5.,Cao Y, Qiu T, Kathayat RS, Azizi SA, Thorne AK, Ahn D, Fukata Y, Fukata M, Rice PA, Dickinson BC Nat Chem Biol. 2019 Dec;15(12):1232-1240. doi: 10.1038/s41589-019-0399-y. Epub, 2019 Nov 18. PMID:31740833<ref>PMID:31740833</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Cao | + | <div class="pdbe-citations 6ny9" style="background-color:#fffaf0;"></div> |
| - | [[Category: Dickinson | + | == References == |
| - | [[Category: Rice | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Cao Y]] | ||
| + | [[Category: Dickinson BC]] | ||
| + | [[Category: Rice PA]] | ||
Current revision
Alpha/beta hydrolase domain-containing protein 10 from mouse
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