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| | <StructureSection load='5ojn' size='340' side='right'caption='[[5ojn]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5ojn' size='340' side='right'caption='[[5ojn]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ojn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OJN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OJN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ojn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OJN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9X8:thioacetyl-ADP-ribose'>9X8</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ojo|5ojo]], [[5oj7|5oj7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9X8:thioacetyl-ADP-ribose'>9X8</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ojn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ojn OCA], [http://pdbe.org/5ojn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ojn RCSB], [http://www.ebi.ac.uk/pdbsum/5ojn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ojn ProSAT]</span></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=5ojn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ojn OCA], [https://pdbe.org/5ojn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ojn RCSB], [https://www.ebi.ac.uk/pdbsum/5ojn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ojn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q28CB4_XENTR Q28CB4_XENTR]] NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues.[HAMAP-Rule:MF_03161] | + | [https://www.uniprot.org/uniprot/Q28CB4_XENTR Q28CB4_XENTR] NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues.[HAMAP-Rule:MF_03161] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pannek, M]] | + | [[Category: Xenopus tropicalis]] |
| - | [[Category: Steegborn, C]] | + | [[Category: Pannek M]] |
| - | [[Category: Deacylase]] | + | [[Category: Steegborn C]] |
| - | [[Category: Mitochondria]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Sirt4]]
| + | |
| - | [[Category: Sirtuin]]
| + | |
| Structural highlights
Function
Q28CB4_XENTR NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues.[HAMAP-Rule:MF_03161]
Publication Abstract from PubMed
Sirtuins are evolutionary conserved NAD(+)-dependent protein lysine deacylases. The seven human isoforms, Sirt1-7, regulate metabolism and stress responses and are considered therapeutic targets for aging-related diseases. Sirt4 locates to mitochondria and regulates fatty acid metabolism and apoptosis. In contrast to the mitochondrial deacetylase Sirt3 and desuccinylase Sirt5, no prominent deacylase activity and structural information are available for Sirt4. Here we describe acyl substrates and crystal structures for Sirt4. The enzyme shows isoform-specific acyl selectivity, with significant activity against hydroxymethylglutarylation. Crystal structures of Sirt4 from Xenopus tropicalis reveal a particular acyl binding site with an additional access channel, rationalizing its activities. The structures further identify a conserved, isoform-specific Sirt4 loop that folds into the active site to potentially regulate catalysis. Using these results, we further establish efficient Sirt4 activity assays, an unusual Sirt4 regulation by NADH, and Sirt4 effects of pharmacological modulators.
Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features.,Pannek M, Simic Z, Fuszard M, Meleshin M, Rotili D, Mai A, Schutkowski M, Steegborn C Nat Commun. 2017 Nov 15;8(1):1513. doi: 10.1038/s41467-017-01701-2. PMID:29138502[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pannek M, Simic Z, Fuszard M, Meleshin M, Rotili D, Mai A, Schutkowski M, Steegborn C. Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features. Nat Commun. 2017 Nov 15;8(1):1513. doi: 10.1038/s41467-017-01701-2. PMID:29138502 doi:http://dx.doi.org/10.1038/s41467-017-01701-2
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