5ytk: Difference between revisions
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==Crystal structure of SIRT3 bound to a leucylated AceCS2== | |||
<StructureSection load='5ytk' size='340' side='right'caption='[[5ytk]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ytk]] is a 10 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=5YTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YTK 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=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</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'>[https://proteopedia.org/fgij/fg.htm?mol=5ytk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ytk OCA], [https://pdbe.org/5ytk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ytk RCSB], [https://www.ebi.ac.uk/pdbsum/5ytk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ytk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SIR3_HUMAN SIR3_HUMAN] NAD-dependent protein deacetylase. Activates mitochondrial target proteins, including ACSS1, IDH2 and GDH by deacetylating key lysine residues. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels.<ref>PMID:16788062</ref> <ref>PMID:18680753</ref> <ref>PMID:18794531</ref> <ref>PMID:19535340</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Amino acids are known regulators of cellular signaling and physiology, but how they are sensed intracellularly is not fully understood. Herein, we report that each aminoacyl-tRNA synthetase (ARS) senses its cognate amino acid sufficiency through catalyzing the formation of lysine aminoacylation (K-AA) on its specific substrate proteins. At physiologic levels, amino acids promote ARSs bound to their substrates and form K-AAs on the varepsilon-amine of lysines in their substrates by producing reactive aminoacyl adenylates. The K-AA marks can be removed by deacetylases, such as SIRT1 and SIRT3, employing the same mechanism as that involved in deacetylation. These dynamically regulated K-AAs transduce signals of their respective amino acids. Reversible leucylation on ras-related GTP-binding protein A/B regulates activity of the mammalian target of rapamycin complex 1. Glutaminylation on apoptosis signal-regulating kinase 1 suppresses apoptosis. We discovered non-canonical functions of ARSs and revealed systematic and functional amino acid sensing and signal transduction networks. | |||
Sensing and Transmitting Intracellular Amino Acid Signals through Reversible Lysine Aminoacylations.,He XD, Gong W, Zhang JN, Nie J, Yao CF, Guo FS, Lin Y, Wu XH, Li F, Li J, Sun WC, Wang ED, An YP, Tang HR, Yan GQ, Yang PY, Wei Y, Mao YZ, Lin PC, Zhao JY, Xu Y, Xu W, Zhao SM Cell Metab. 2017 Nov 27. pii: S1550-4131(17)30629-0. doi:, 10.1016/j.cmet.2017.10.015. PMID:29198988<ref>PMID:29198988</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ytk" style="background-color:#fffaf0;"></div> | ||
[[Category: Gong | |||
[[Category: Xu | ==See Also== | ||
*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Gong W]] | |||
[[Category: Li J]] | |||
[[Category: Xu Y]] | |||
Latest revision as of 11:37, 22 November 2023
Crystal structure of SIRT3 bound to a leucylated AceCS2Crystal structure of SIRT3 bound to a leucylated AceCS2
Structural highlights
FunctionSIR3_HUMAN NAD-dependent protein deacetylase. Activates mitochondrial target proteins, including ACSS1, IDH2 and GDH by deacetylating key lysine residues. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels.[1] [2] [3] [4] Publication Abstract from PubMedAmino acids are known regulators of cellular signaling and physiology, but how they are sensed intracellularly is not fully understood. Herein, we report that each aminoacyl-tRNA synthetase (ARS) senses its cognate amino acid sufficiency through catalyzing the formation of lysine aminoacylation (K-AA) on its specific substrate proteins. At physiologic levels, amino acids promote ARSs bound to their substrates and form K-AAs on the varepsilon-amine of lysines in their substrates by producing reactive aminoacyl adenylates. The K-AA marks can be removed by deacetylases, such as SIRT1 and SIRT3, employing the same mechanism as that involved in deacetylation. These dynamically regulated K-AAs transduce signals of their respective amino acids. Reversible leucylation on ras-related GTP-binding protein A/B regulates activity of the mammalian target of rapamycin complex 1. Glutaminylation on apoptosis signal-regulating kinase 1 suppresses apoptosis. We discovered non-canonical functions of ARSs and revealed systematic and functional amino acid sensing and signal transduction networks. Sensing and Transmitting Intracellular Amino Acid Signals through Reversible Lysine Aminoacylations.,He XD, Gong W, Zhang JN, Nie J, Yao CF, Guo FS, Lin Y, Wu XH, Li F, Li J, Sun WC, Wang ED, An YP, Tang HR, Yan GQ, Yang PY, Wei Y, Mao YZ, Lin PC, Zhao JY, Xu Y, Xu W, Zhao SM Cell Metab. 2017 Nov 27. pii: S1550-4131(17)30629-0. doi:, 10.1016/j.cmet.2017.10.015. PMID:29198988[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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