1U35

Crystal structure of the nucleosome core particle containing the histone domain of macroH2A

Summary for 1U35

• Entry DOI: 10.2210/pdb1u35/pdb
• Related: 1AOI 1F66
• Descriptor: alpha-satellite DNA, Histone H3.1, Hist1h4i protein, ... (6 entities in total)
• Functional Keywords: nucleosome, ncp, histone fold, histone variant, macroh2a, structural protein-dna complex, structural protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P68433 O75367 Q9D2U9
• Total number of polymer chains: 10
• Total formula weight: 197792.12

Authors

Chakravarthy, S.,Gundimella, S.K.,Caron, C.,Perche, P.Y.,Pehrson, J.R.,Khochbin, S.,Luger, K. (deposition date: 2004-07-20, release date: 2005-09-27, Last modification date: 2023-08-23)

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 (3 Å)