4uu7: Difference between revisions

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-'''Unreleased structure'''
+==Crystal structure of zebrafish Sirtuin 5 in complex with 3-methyl- succinylated CPS1-peptide==
+<StructureSection load='4uu7' size='340' side='right' caption='[[4uu7]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4uu7]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UU7 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=JO3:(2R)-2-METHYLBUTANEDIOIC+ACID'>JO3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SUH:(2S)-2-METHYLBUTANEDIOIC+ACID'>SUH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
+<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene></td></tr>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4utn|4utn]], [[4utr|4utr]], [[4utv|4utv]], [[4utx|4utx]], [[4utz|4utz]], [[4uu8|4uu8]], [[4uua|4uua]], [[4uub|4uub]]</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uu7 RCSB], [http://www.ebi.ac.uk/pdbsum/4uu7 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Sirtuins are NAD+ -dependent deacetylases acting as sensors in metabolic pathways and stress response. In mammals there are seven isoforms. The mitochondrial sirtuin 5 is a weak deacetylase but a very efficient demalonylase and desuccinylase; however, its substrate acyl specificity has not been systematically analyzed. Herein, we investigated a carbamoyl phosphate synthetase 1 derived peptide substrate and modified the lysine side chain systematically to determine the acyl specificity of Sirt5. From that point we designed six potent peptide-based inhibitors that interact with the NAD+ binding pocket. To characterize the interaction details causing the different substrate and inhibition properties we report several X-ray crystal structures of Sirt5 complexed with these peptides. Our results reveal the Sirt5 acyl selectivity and its molecular basis and enable the design of inhibitors for Sirt5.
-The entry 4uu7 is ON HOLD  until Paper Publication
+Chemical Probing of the Human Sirtuin 5 Active Site Reveals Its Substrate Acyl Specificity and Peptide-Based Inhibitors.,Roessler C, Nowak T, Pannek M, Gertz M, Nguyen GT, Scharfe M, Born I, Sippl W, Steegborn C, Schutkowski M Angew Chem Int Ed Engl. 2014 Aug 11. doi: 10.1002/anie.201402679. PMID:25111069<ref>PMID:25111069</ref>
-Authors: Pannek, M., Gertz, M., Steegborn, C.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of zebrafish Sirtuin 5 in complex with 3-methyl-succinylated CPS1-peptide
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gertz, M.]]
+[[Category: Pannek, M.]]
+[[Category: Steegborn, C.]]
+[[Category: Deacylase]]
+[[Category: Hydrolase]]
+[[Category: Mitochondrial]]
+[[Category: Regulatory enzyme]]
+[[Category: Rossmann-fold]]
+[[Category: Sirtuin 5]]
+[[Category: Zinc-binding]]