3tu4
From Proteopedia
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| - | [[ | + | ==Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.== |
| + | <StructureSection load='3tu4' size='340' side='right' caption='[[3tu4]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TU4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hist1h2aj, LOC494591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), 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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [http://www.ebi.ac.uk/pdbsum/3tu4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component. | ||
| - | + | Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution.,Armache KJ, Garlick JD, Canzio D, Narlikar GJ, Kingston RE Science. 2011 Nov 18;334(6058):977-82. PMID:22096199<ref>PMID:22096199</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Histone|Histone]] | *[[Histone|Histone]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
| - | [[Category: Armache, K J | + | [[Category: Armache, K J]] |
| - | [[Category: Canzio, D | + | [[Category: Canzio, D]] |
| - | [[Category: Garlick, J D | + | [[Category: Garlick, J D]] |
| - | [[Category: Kingston, R E | + | [[Category: Kingston, R E]] |
| - | [[Category: Narlikar, G J | + | [[Category: Narlikar, G J]] |
[[Category: Gene silencing]] | [[Category: Gene silencing]] | ||
[[Category: Histone]] | [[Category: Histone]] | ||
[[Category: Nucleosome]] | [[Category: Nucleosome]] | ||
[[Category: Signaling protein-structural protein-dna complex]] | [[Category: Signaling protein-structural protein-dna complex]] | ||
Revision as of 16:39, 9 December 2014
Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.
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