1f66
|
2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z
OverviewOverview
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 StructureAbout this Structure
1F66 is a Protein complex structure of sequences from Homo sapiens, Mus musculus and Xenopus laevis with MN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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 Mon Nov 12 16:49:41 2007