4kui
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of N-terminal acetylated yeast Sir3 BAH domain== | |
- | + | <StructureSection load='4kui' size='340' side='right' caption='[[4kui]], [[Resolution|resolution]] 1.85Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[4kui]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KUI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KUI FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr> | ||
+ | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kud|4kud]], [[4kul|4kul]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kui OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kui RCSB], [http://www.ebi.ac.uk/pdbsum/4kui PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | In Saccharomyces cerevisiae, acetylation of the Sir3 N terminus is important for transcriptional silencing. This covalent modification promotes the binding of the Sir3 BAH domain to the nucleosome, but a mechanistic understanding of this phenomenon is lacking. By X-ray crystallography, we show here that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain. | ||
- | + | Nalpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.,Yang D, Fang Q, Wang M, Ren R, Wang H, He M, Sun Y, Yang N, Xu RM Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2637. PMID:23934152<ref>PMID:23934152</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
- | [[Category: Fang, Q | + | [[Category: Fang, Q]] |
- | [[Category: He, M | + | [[Category: He, M]] |
- | [[Category: Ren, R | + | [[Category: Ren, R]] |
- | [[Category: Sun, Y | + | [[Category: Sun, Y]] |
- | [[Category: Wang, H | + | [[Category: Wang, H]] |
- | [[Category: Wang, M | + | [[Category: Wang, M]] |
- | [[Category: Xu, R M | + | [[Category: Xu, R M]] |
- | [[Category: Yang, D | + | [[Category: Yang, D]] |
- | [[Category: Yang, N | + | [[Category: Yang, N]] |
[[Category: Bah domain]] | [[Category: Bah domain]] | ||
[[Category: Nucleus]] | [[Category: Nucleus]] | ||
[[Category: Silencing]] | [[Category: Silencing]] | ||
[[Category: Transcription]] | [[Category: Transcription]] |
Revision as of 14:54, 21 December 2014
Crystal structure of N-terminal acetylated yeast Sir3 BAH domain
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Categories: Saccharomyces cerevisiae s288c | Fang, Q | He, M | Ren, R | Sun, Y | Wang, H | Wang, M | Xu, R M | Yang, D | Yang, N | Bah domain | Nucleus | Silencing | Transcription