Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)

Structural highlights

2fxk is a 2 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 1zq0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Evolutionary Conservation

 

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Publication Abstract from PubMed

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.

Splicing regulates NAD metabolite binding to histone macroH2A.,Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG Nat Struct Mol Biol. 2005 Jul;12(7):624-5. Epub 2005 Jun 19. PMID:15965484[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG. Splicing regulates NAD metabolite binding to histone macroH2A. Nat Struct Mol Biol. 2005 Jul;12(7):624-5. Epub 2005 Jun 19. PMID:15965484 doi:http://dx.doi.org/10.1038/nsmb956

2fxk, resolution 2.54Å

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