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1f66

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1f66, resolution 2.60Å ()
Ligands:
Domains: H2A, H4, H3, H2B
Related: 1aoi
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1F66 is a 10 chains structure of sequences from Homo sapiens, Mus musculus and Xenopus laevis. Full crystallographic information is available from OCA.

Reference

  • Suto RK, Clarkson MJ, Tremethick DJ, Luger K. Crystal structure of a nucleosome core particle containing the variant histone H2A.Z. Nat Struct Biol. 2000 Dec;7(12):1121-4. PMID:11101893 doi:10.1038/81971

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