2g3r
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Crystal Structure of 53BP1 tandem tudor domains at 1.2 A resolution
OverviewOverview
Histone lysine methylation has been linked to the recruitment of mammalian, DNA repair factor 53BP1 and putative fission yeast homolog Crb2 to DNA, double-strand breaks (DSBs), but how histone recognition is achieved has, not been established. Here we demonstrate that this link occurs through, direct binding of 53BP1 and Crb2 to histone H4. Using X-ray, crystallography and nuclear magnetic resonance (NMR) spectroscopy, we show, that, despite low amino acid sequence conservation, both 53BP1 and Crb2, contain tandem tudor domains that interact with histone H4 specifically, dimethylated at Lys20 (H4-K20me2). The structure of 53BP1/H4-K20me2, complex uncovers a unique five-residue 53BP1 binding cage, remarkably, conserved in the structure of Crb2, that best accommodates a, dimethyllysine but excludes a trimethyllysine, thus explaining the, methylation state-specific recognition of H4-K20. This study reveals an, evolutionarily conserved molecular mechanism of targeting DNA repair, proteins to DSBs by direct recognition of H4-K20me2.
About this StructureAbout this Structure
2G3R is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair., Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, Chen J, Mer G, Cell. 2006 Dec 29;127(7):1361-73. PMID:17190600
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