4ld9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle== | |
| + | <StructureSection load='4ld9' size='340' side='right'caption='[[4ld9]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ld9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LD9 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]] 3.306Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=4ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld9 OCA], [https://pdbe.org/4ld9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ld9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ld9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis. | ||
| - | + | The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.,Arnaudo N, Fernandez IS, McLaughlin SH, Peak-Chew SY, Rhodes D, Martino F Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2641. PMID:23934150<ref>PMID:23934150</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4ld9" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Histone 3D structures|Histone 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Arnaudo N]] | ||
| + | [[Category: Fernandez IS]] | ||
| + | [[Category: Martino F]] | ||
| + | [[Category: McLaughlin SH]] | ||
| + | [[Category: Peak-Chew SY]] | ||
| + | [[Category: Rhodes D]] | ||
Current revision
Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle
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