|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Structural and functional analysis of ada2 alpha swirm domain== | | ==Structural and functional analysis of ada2 alpha swirm domain== |
| - | <StructureSection load='2aqe' size='340' side='right' caption='[[2aqe]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2aqe' size='340' side='right'caption='[[2aqe]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2aqe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AQE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2aqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AQE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2aqf|2aqf]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tada21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=2aqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aqe OCA], [https://pdbe.org/2aqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aqe RCSB], [https://www.ebi.ac.uk/pdbsum/2aqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aqe ProSAT]</span></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=2aqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aqe OCA], [http://pdbe.org/2aqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aqe RCSB], [http://www.ebi.ac.uk/pdbsum/2aqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aqe ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TAD2A_MOUSE TAD2A_MOUSE]] Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling (By similarity). | + | [https://www.uniprot.org/uniprot/TAD2A_MOUSE TAD2A_MOUSE] Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Qian, C]] | + | [[Category: Mus musculus]] |
| - | [[Category: Zeng, L]] | + | [[Category: Qian C]] |
| - | [[Category: Zhang, Q]] | + | [[Category: Zeng L]] |
| - | [[Category: Zhou, M M]] | + | [[Category: Zhang Q]] |
| - | [[Category: Helix-turn-helix]]
| + | [[Category: Zhou M-M]] |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
TAD2A_MOUSE Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2alpha. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2alpha and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2alpha SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling.
Structure and chromosomal DNA binding of the SWIRM domain.,Qian C, Zhang Q, Li S, Zeng L, Walsh MJ, Zhou MM Nat Struct Mol Biol. 2005 Dec;12(12):1078-85. Epub 2005 Nov 20. PMID:16299514[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qian C, Zhang Q, Li S, Zeng L, Walsh MJ, Zhou MM. Structure and chromosomal DNA binding of the SWIRM domain. Nat Struct Mol Biol. 2005 Dec;12(12):1078-85. Epub 2005 Nov 20. PMID:16299514 doi:10.1038/nsmb1022
|
