1zr5

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Image:1zr5.gif


PDB ID 1zr5

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, resolution 2.92Å
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1ZR5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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