1ZR5

Crystal structure of the macro-domain of human core histone variant macroH2A1.2

Summary for 1ZR5

• Entry DOI: 10.2210/pdb1zr5/pdb
• Related: 1ZQ0 1ZR3
• Descriptor: H2AFY protein (2 entities in total)
• Functional Keywords: chromatin, histone, a1pp, macro-domain, p-loop, splicing, gene regulation
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: O75367
• Total number of polymer chains: 2
• Total formula weight: 45413.73

Authors

Kustatscher, G.,Hothorn, M.,Pugieux, C.,Scheffzek, K.,Ladurner, A.G. (deposition date: 2005-05-19, release date: 2005-06-21, Last modification date: 2023-08-23)

Primary citation

Kustatscher, G.,Hothorn, M.,Pugieux, C.,Scheffzek, K.,Ladurner, A.G.
Splicing regulates NAD metabolite binding to histone macroH2A.
Nat.Struct.Mol.Biol., 12:624-625, 2005

PubMed Abstract: Histone macroH2A is a hallmark of mammalian heterochromatin. Here we show that human macroH2A1.1 binds the SirT1-metabolite O-acetyl-ADP-ribose (OAADPR) through its macro domain. The 1.6-A crystal structure and mutants reveal how the metabolite is recognized. Mutually exclusive exon use in the gene H2AFY produces macroH2A1.2, whose tissue distribution differs. MacroH2A1.2 shows only subtle structural changes but cannot bind nucleotides. Alternative splicing may thus regulate the binding of nicotinamide adenine dinucleotide (NAD) metabolites to chromatin.

PubMed: 15965484
DOI: 10.1038/nsmb956

Experimental method

X-RAY DIFFRACTION (2.92 Å)