4ld9: Difference between revisions
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==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle== | ==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=''> | <StructureSection load='4ld9' size='340' side='right'caption='[[4ld9]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ld9]] is a 12 chain structure with sequence from [ | <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=' | </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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/H32_XENLA H32_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Histone|Histone]] | *[[Histone 3D structures|Histone 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae S288C]] | ||
[[Category: Arnaudo | [[Category: Xenopus laevis]] | ||
[[Category: Fernandez | [[Category: Arnaudo N]] | ||
[[Category: Martino | [[Category: Fernandez IS]] | ||
[[Category: McLaughlin | [[Category: Martino F]] | ||
[[Category: Peak-Chew | [[Category: McLaughlin SH]] | ||
[[Category: Rhodes | [[Category: Peak-Chew SY]] | ||
[[Category: Rhodes D]] | |||