OCA at 08:07, 22 May 2024

2024-05-22T08:07:41Z

←Older revision		Revision as of 08:07, 22 May 2024
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-	'''Unreleased structure'''

-	~~The entry~~ 8xe7 is ~~ON HOLD until Paper~~ Publication	+	==Crystal structure of human Sirt2 without Sirt2-specific insertion==
		+	<StructureSection load='8xe7' size='340' side='right'caption='[[8xe7]], [[Resolution\|resolution]] 1.95Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8xe7]] 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=8XE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XE7 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]] 1.95Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=8xe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xe7 OCA], [https://pdbe.org/8xe7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xe7 RCSB], [https://www.ebi.ac.uk/pdbsum/8xe7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xe7 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/SIR2_HUMAN SIR2_HUMAN] NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA.<ref>PMID:12620231</ref> <ref>PMID:12697818</ref> <ref>PMID:21081649</ref> <ref>PMID:21726808</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Sirtuin 2 (SIRT2) is a class III histone deacetylase that is highly conserved from bacteria to mammals. We prepared and characterized the wild-type (WT) and mutant forms of the histone deacetylase (HDAC) domain of human SIRT2 (hSIRT2) using various biophysical methods and evaluated their deacetylation activity. We found that WT hSIRT2 HDAC (residues 52-357) forms a homodimer in a concentration-dependent manner with a dimer-monomer dissociation constant of 8.3 +/- 0.5 muM, which was determined by mass spectrometry. The dimer was disrupted into two monomers by binding to the HDAC inhibitors SirReal1 and SirReal2. We also confirmed dimer formation of hSIRT2 HDAC in living cells using a NanoLuc complementation reporter system. Examination of the relationship between dimer formation and deacetylation activity using several mutants of hSIRT2 HDAC revealed that some non-dimerizing mutants exhibited deacetylation activity for the N-terminal peptide of histone H3, similar to the wild type. The hSIRT2 HDAC mutant Delta292-306, which lacks a SIRT2-specific disordered loop region, was identified to exist as a monomer with slightly reduced deacetylation activity; the X-ray structure of the mutant Delta292-306 was almost identical to that of the WT hSIRT2 HDAC bound to an inhibitor. These results indicate that hSIRT2 HDAC forms a dimer, but this is independent of deacetylation activity. Herein, we discuss insights into the dimer formation of hSIRT2 based on our biophysical experimental results.

-	~~Authors~~:	+	Biophysical insights into the dimer formation of human Sirtuin 2.,Suzuki N, Konuma T, Ikegami T, Akashi S Protein Sci. 2024 May;33(5):e4994. doi: 10.1002/pro.4994. PMID:38647411<ref>PMID:38647411</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8xe7" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Akashi S]]
		+	[[Category: Konuma T]]

OCA at 09:09, 17 January 2024

2024-01-17T09:09:09Z

←Older revision		Revision as of 09:09, 17 January 2024
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8xe7 is ON HOLD	+	The entry 8xe7 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8xe7" [edit=sysop:move=sysop]

2023-12-20T09:08:42Z

Protected "8xe7" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:08, 20 December 2023

OCA: New page: '''Unreleased structure''' The entry 8xe7 is ON HOLD Authors: Description: Category: Unreleased Structures

2023-12-20T09:08:41Z

New page: '''Unreleased structure''' The entry 8xe7 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8xe7 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]

8xe7 - Revision history

OCA at 08:07, 22 May 2024

OCA at 09:09, 17 January 2024

OCA: Protected "8xe7" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 8xe7 is ON HOLD Authors: Description: Category: Unreleased Structures