Summary information and primary citation
- PDB-id
-
1u35;
SNAP-derived features in text and
JSON formats
- 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.
