1F66

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

Summary for 1F66

• Entry DOI: 10.2210/pdb1f66/pdb
• Related: 1AOI
• Descriptor: PALINDROMIC 146 BASE PAIR DNA FRAGMENT, HISTONE H3, HISTONE H4, ... (7 entities in total)
• Functional Keywords: nucleosome, chromatin, histone, histone variant, protein dna interaction, nucleoprotein, supercoiled dna, complex (nucleosome core-dna), structural protein-dna complex, structural protein/dna
• Biological source: Xenopus laevis (African clawed frog); More
• Cellular location: Nucleus (By similarity): P62806; Nucleus: P17317 P02281
• Total number of polymer chains: 10
• Total formula weight: 199859.16

Authors

Suto, R.K.,Clarkson, M.J.,Tremethick, D.J.,Luger, K. (deposition date: 2000-06-20, release date: 2000-11-27, Last modification date: 2024-02-07)

Primary citation

Suto, R.K.,Clarkson, M.J.,Tremethick, D.J.,Luger, K.
Crystal structure of a nucleosome core particle containing the variant histone H2A.Z.
Nat.Struct.Biol., 7:1121-1124, 2000

PubMed Abstract: 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.

PubMed: 11101893
DOI: 10.1038/81971

Experimental method

X-RAY DIFFRACTION (2.6 Å)