1YD9

1.6A Crystal Structure of the Non-Histone Domain of the Histone Variant MacroH2A1.1.

Summary for 1YD9

• Entry DOI: 10.2210/pdb1yd9/pdb
• Related: 1BFR 1HJZ 1VHU
• Descriptor: Core histone macro-H2A.1, GOLD ION (3 entities in total)
• Functional Keywords: alpha-beta structure, a1pp domain, macro-domain, structural protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Nucleus (By similarity): Q02874
• Total number of polymer chains: 4
• Total formula weight: 82941.95

Authors

Chakravarthy, S.,Swamy, G.Y.S.K.,Caron, C.,Perche, P.Y.,Pehrson, J.R.,Khochbin, S.,Luger, K. (deposition date: 2004-12-23, release date: 2005-09-27, Last modification date: 2024-02-14)

Primary citation

Chakravarthy, S.,Gundimella, S.K.,Caron, C.,Perche, P.Y.,Pehrson, J.R.,Khochbin, S.,Luger, K.
Structural characterization of the histone variant macroH2A
Mol.Cell.Biol., 25:7616-7624, 2005

PubMed 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.

PubMed: 16107708
DOI: 10.1128/MCB.25.17.7616-7624.2005

Experimental method

X-RAY DIFFRACTION (1.6 Å)