1f66
From Proteopedia
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| - | [[Image:1f66.gif|left|200px]] | + | [[Image:1f66.gif|left|200px]] |
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| - | '''2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z''' | + | {{Structure |
| + | |PDB= 1f66 |SIZE=350|CAPTION= <scene name='initialview01'>1f66</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F66 is a [ | + | 1F66 is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F66 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11101893 11101893] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: supercoiled dna]] | [[Category: supercoiled dna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:05:01 2008'' |
Revision as of 09:05, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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