6rxm
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of CobB Ac2 (A76G, I131C, V162G) in complex with H4K16-Acetyl peptide== | |
| + | <StructureSection load='6rxm' size='340' side='right'caption='[[6rxm]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RXM 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]] 1.92Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</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=6rxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rxm OCA], [https://pdbe.org/6rxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rxm RCSB], [https://www.ebi.ac.uk/pdbsum/6rxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rxm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lysine acylations, a family of diverse protein modifications varying in acyl group length, charge and saturation, are linked to many important physiological processes. Only a small set of substrate-promiscuous lysine acetyltransferases and deacetylases (KDACs) install and remove this vast variety of modifications. Engineered KDACs that remove only one type of acylation would help to dissect the different contributions of distinct acylations to cell physiology. Therefore, we developed a bacterial selection system for the directed evolution of KDACs with which we identified variants up to 400 times more selective for butyryl- compared to crotonyl-lysine. Structural analyses revealed that the enzyme adopts different conformational states depending on the type of acylation of the bound peptide. We used the butyryl-selective KDAC variant to shift the cellular acylation spectrum towards increased lysine crotonylation. Hence, these new enzymes will help dissecting the different roles of lysine acylations in cell physiology. | ||
| - | + | Evolved, Selective Erasers of Distinct Lysine Acylations.,Spinck M, Neumann-Staubitz P, Ecke M, Gasper R, Neumann H Angew Chem Int Ed Engl. 2020 Mar 18. doi: 10.1002/anie.202002899. PMID:32187803<ref>PMID:32187803</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Gasper | + | <div class="pdbe-citations 6rxm" style="background-color:#fffaf0;"></div> |
| - | [[Category: Neumann | + | == References == |
| - | [[Category: Spinck | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gasper R]] | ||
| + | [[Category: Neumann H]] | ||
| + | [[Category: Spinck M]] | ||
Current revision
Crystal structure of CobB Ac2 (A76G, I131C, V162G) in complex with H4K16-Acetyl peptide
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