1yd9
From Proteopedia
(New page: 200px<br /><applet load="1yd9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yd9, resolution 1.6Å" /> '''1.6A Crystal Structur...) |
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| - | [[Image:1yd9.gif|left|200px]]<br /><applet load="1yd9" size=" | + | [[Image:1yd9.gif|left|200px]]<br /><applet load="1yd9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yd9, resolution 1.6Å" /> | caption="1yd9, resolution 1.6Å" /> | ||
'''1.6A Crystal Structure of the Non-Histone Domain of the Histone Variant MacroH2A1.1.'''<br /> | '''1.6A Crystal Structure of the Non-Histone Domain of the Histone Variant MacroH2A1.1.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | macroH2A is an H2A variant with a highly unusual structural organization. | + | macroH2A is an H2A variant with a highly unusual structural organization. It has a C-terminal domain connected to the N-terminal histone domain by a linker. Crystallographic and biochemical studies show that changes in the L1 loop in the histone fold region of macroH2A impact the structure and potentially the function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region reveals an alpha/beta fold which has previously been found in a functionally diverse group of proteins. This region associates with histone deacetylases and affects the acetylation status of nucleosomes containing macroH2A. Thus, the unusual domain structure of macroH2A integrates independent functions that are instrumental in establishing a structurally and functionally unique chromatin domain. |
==About this Structure== | ==About this Structure== | ||
| - | 1YD9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with AU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YD9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=AU:'>AU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YD9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Khochbin, S.]] | [[Category: Khochbin, S.]] | ||
[[Category: Luger, K.]] | [[Category: Luger, K.]] | ||
| - | [[Category: Pehrson, J | + | [[Category: Pehrson, J R.]] |
| - | [[Category: Perche, P | + | [[Category: Perche, P Y.]] |
| - | [[Category: Swamy, G | + | [[Category: Swamy, G Y.S K.]] |
[[Category: AU]] | [[Category: AU]] | ||
[[Category: a1pp domain]] | [[Category: a1pp domain]] | ||
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[[Category: macro-domain]] | [[Category: macro-domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:10 2008'' |
Revision as of 14:04, 21 February 2008
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1.6A Crystal Structure of the Non-Histone Domain of the Histone Variant MacroH2A1.1.
Overview
macroH2A is an H2A variant with a highly unusual structural organization. It has a C-terminal domain connected to the N-terminal histone domain by a linker. Crystallographic and biochemical studies show that changes in the L1 loop in the histone fold region of macroH2A impact the structure and potentially the function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region reveals an alpha/beta fold which has previously been found in a functionally diverse group of proteins. This region associates with histone deacetylases and affects the acetylation status of nucleosomes containing macroH2A. Thus, the unusual domain structure of macroH2A integrates independent functions that are instrumental in establishing a structurally and functionally unique chromatin domain.
About this Structure
1YD9 is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural characterization of the histone variant macroH2A., Chakravarthy S, Gundimella SK, Caron C, Perche PY, Pehrson JR, Khochbin S, Luger K, Mol Cell Biol. 2005 Sep;25(17):7616-24. PMID:16107708
Page seeded by OCA on Thu Feb 21 16:04:10 2008
