5ytk: Difference between revisions

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'''Unreleased structure'''


The entry 5ytk is ON HOLD  until Paper Publication
==Crystal structure of SIRT3 bound to a leucylated AceCS2==
 
<StructureSection load='5ytk' size='340' side='right' caption='[[5ytk]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
Authors: Li, J., Gong, W., Xu, Y.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5ytk]] is a 10 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YTK FirstGlance]. <br>
Description: Crystal structure of SIRT3 bound to a leucylated AceCS2
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ytk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ytk OCA], [http://pdbe.org/5ytk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ytk RCSB], [http://www.ebi.ac.uk/pdbsum/5ytk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ytk ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gong, W]]
[[Category: Li, J]]
[[Category: Li, J]]
[[Category: Gong, W]]
[[Category: Xu, Y]]
[[Category: Xu, Y]]
[[Category: Dna-dependent deacetylase sirtuin-3]]
[[Category: Hydrolase]]
[[Category: Leucylated acecs2]]

Revision as of 11:35, 27 December 2017

Crystal structure of SIRT3 bound to a leucylated AceCS2Crystal structure of SIRT3 bound to a leucylated AceCS2

Structural highlights

5ytk is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1] [2] [3] [4]

References

  1. ↑ Schwer B, Bunkenborg J, Verdin RO, Andersen JS, Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10224-9. Epub 2006 Jun 20. PMID:16788062 doi:10.1073/pnas.0603968103
  2. ↑ Schlicker C, Gertz M, Papatheodorou P, Kachholz B, Becker CF, Steegborn C. Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J Mol Biol. 2008 Oct 10;382(3):790-801. doi: 10.1016/j.jmb.2008.07.048. Epub 2008, Jul 25. PMID:18680753 doi:10.1016/j.jmb.2008.07.048
  3. ↑ Ahn BH, Kim HS, Song S, Lee IH, Liu J, Vassilopoulos A, Deng CX, Finkel T. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14447-52. doi:, 10.1073/pnas.0803790105. Epub 2008 Sep 15. PMID:18794531 doi:10.1073/pnas.0803790105
  4. ↑ Jin L, Wei W, Jiang Y, Peng H, Cai J, Mao C, Dai H, Choy W, Bemis JE, Jirousek MR, Milne JC, Westphal CH, Perni RB. Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J Biol Chem. 2009 Sep 4;284(36):24394-405. Epub 2009 Jun 16. PMID:19535340 doi:10.1074/jbc.M109.014928

5ytk, resolution 2.70Å

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