2aqf

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(New page: 200px<br /><applet load="2aqf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aqf" /> '''Structural and functional analysis of ADA2 a...)
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[[Image:2aqf.gif|left|200px]]<br /><applet load="2aqf" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="2aqf" />
'''Structural and functional analysis of ADA2 alpha swirm domain'''<br />
'''Structural and functional analysis of ADA2 alpha swirm domain'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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2AQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AQF OCA].
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2AQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AQF OCA].
==Reference==
==Reference==
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[[Category: Zeng, L.]]
[[Category: Zeng, L.]]
[[Category: Zhang, Q.]]
[[Category: Zhang, Q.]]
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[[Category: Zhou, M.M.]]
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[[Category: Zhou, M M.]]
[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:17:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:29:50 2008''

Revision as of 14:29, 21 February 2008


2aqf

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Structural and functional analysis of ADA2 alpha swirm domain

Overview

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.

About this Structure

2AQF is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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

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