ISDA: 2FXK

Deposition Date 2006-02-06

Release Date 2006-02-14

Last Version Date 2023-08-30

Entry Detail

PDB ID:

2FXK

Keywords:

GENE REGULATION

Title:

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

Biological Source:

Source Organism(s):

Homo sapiens (Taxon ID: 9606)

Expression System(s):

Escherichia coli bl21(de3)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.54 Å

R-Value Free:

0.27

R-Value Work:

0.20

R-Value Observed:

0.21

Space Group:

P 21 21 2

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:H2A histone family, member Y
Mutagens:non-histone macro-domain (Residues: 182-369)
Chain IDs:A, B
Chain Length:211
Number of Molecules:2
Biological Source:Homo sapiens

UniProt ID:O75367 Pfam ID:PF01661

Primary Citation

Splicing regulates NAD metabolite binding to histone macroH2A.

Kustatscher, G, Hothorn, M, Pugieux, C, Scheffzek, K, Ladurner, A.G.Show

Nat. Struct. Mol. Biol. 12 624 625 (2005)

PMID: 15965484 DOI: 10.1038/nsmb956

Abstact

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.

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Primary Citation of related structures

Abstact

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