SNAP output for PDB entry 1u35 [SNAP web server]

PDB-id

1u35; SNAP-derived features in text and JSON formats; DNAproDB

Class

structural protein-DNA

Method

X-ray (3.0 Å)

Summary

Crystal structure of the nucleosome core particle containing the histone domain of macroh2a

Reference

Chakravarthy S, Gundimella SK, Caron C, Perche PY, Pehrson JR, Khochbin S, Luger K (2005): "Structural characterization of the histone variant macroH2A." Mol.Cell.Biol., 25, 7616-7624. doi: 10.1128/MCB.25.17.7616-7624.2005.

Abstract

macroH2A is an H2A variant with a highly unusual structural organization. It has a C-terminal domain connected to the N-terminal histone domain by a linker. Crystallographic and biochemical studies show that changes in the L1 loop in the histone fold region of macroH2A impact the structure and potentially the function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region reveals an alpha/beta fold which has previously been found in a functionally diverse group of proteins. This region associates with histone deacetylases and affects the acetylation status of nucleosomes containing macroH2A. Thus, the unusual domain structure of macroH2A integrates independent functions that are instrumental in establishing a structurally and functionally unique chromatin domain.