1f66
From Proteopedia
(New page: 200px<br /> <applet load="1f66" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f66, resolution 2.6Å" /> '''2.6 A CRYSTAL STRUCT...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1f66.gif|left|200px]]<br /> | + | [[Image:1f66.gif|left|200px]]<br /><applet load="1f66" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1f66" size=" | + | |
caption="1f66, resolution 2.6Å" /> | caption="1f66, resolution 2.6Å" /> | ||
'''2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z'''<br /> | '''2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Activation of transcription within chromatin has been correlated with the | + | Activation of transcription within chromatin has been correlated with the incorporation of the essential histone variant H2A.Z into nucleosomes. H2A.Z and other histone variants may establish structurally distinct chromosomal domains; however, the molecular mechanism by which they function is largely unknown. Here we report the 2.6 A crystal structure of a nucleosome core particle containing the histone variant H2A.Z. The overall structure is similar to that of the previously reported 2.8 A nucleosome structure containing major histone proteins. However, distinct localized changes result in the subtle destabilization of the interaction between the (H2A.Z-H2B) dimer and the (H3-H4)(2) tetramer. Moreover, H2A.Z nucleosomes have an altered surface that includes a metal ion. This altered surface may lead to changes in higher order structure, and/or could result in the association of specific nuclear proteins with H2A.Z. Finally, incorporation of H2A.Z and H2A within the same nucleosome is unlikely, due to significant changes in the interface between the two H2A.Z-H2B dimers. |
==About this Structure== | ==About this Structure== | ||
| - | 1F66 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1F66 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F66 OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 15: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
| - | [[Category: Clarkson, M | + | [[Category: Clarkson, M J.]] |
[[Category: Luger, K.]] | [[Category: Luger, K.]] | ||
| - | [[Category: Suto, R | + | [[Category: Suto, R K.]] |
| - | [[Category: Tremethick, D | + | [[Category: Tremethick, D J.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: chromatin]] | [[Category: chromatin]] | ||
| Line 30: | Line 29: | ||
[[Category: supercoiled dna]] | [[Category: supercoiled dna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:17 2008'' |
Revision as of 10:35, 21 February 2008
|
2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z
Overview
Activation of transcription within chromatin has been correlated with the incorporation of the essential histone variant H2A.Z into nucleosomes. H2A.Z and other histone variants may establish structurally distinct chromosomal domains; however, the molecular mechanism by which they function is largely unknown. Here we report the 2.6 A crystal structure of a nucleosome core particle containing the histone variant H2A.Z. The overall structure is similar to that of the previously reported 2.8 A nucleosome structure containing major histone proteins. However, distinct localized changes result in the subtle destabilization of the interaction between the (H2A.Z-H2B) dimer and the (H3-H4)(2) tetramer. Moreover, H2A.Z nucleosomes have an altered surface that includes a metal ion. This altered surface may lead to changes in higher order structure, and/or could result in the association of specific nuclear proteins with H2A.Z. Finally, incorporation of H2A.Z and H2A within the same nucleosome is unlikely, due to significant changes in the interface between the two H2A.Z-H2B dimers.
About this Structure
1F66 is a Protein complex structure of sequences from Homo sapiens, Mus musculus and Xenopus laevis with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a nucleosome core particle containing the variant histone H2A.Z., Suto RK, Clarkson MJ, Tremethick DJ, Luger K, Nat Struct Biol. 2000 Dec;7(12):1121-4. PMID:11101893
Page seeded by OCA on Thu Feb 21 12:35:17 2008
