2K3Y
Solution structure of EAF3 chromo barrel domain bound to histone h3 with a dimethyllysine analog H3K36ME2
Summary for 2K3Y
| Entry DOI | 10.2210/pdb2k3y/pdb |
| Descriptor | Chromatin modification-related protein EAF3 (1 entity in total) |
| Functional Keywords | eaf3, dimethylated histone h3k36, eaf3-h3k36me2 fusion, chromo barrel domain, histone deacetylase, chromatin regulator, dna damage, dna repair, nucleus, phosphoprotein, transcription, transcription regulation, chromosomal protein, dna-binding, transcription regulator |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 15367.36 |
| Authors | |
| Primary citation | Xu, C.,Cui, G.,Botuyan, M.V.,Mer, G. Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S. Structure, 16:1740-1750, 2008 Cited by PubMed Abstract: Deacetylation of nucleosomes by the Rpd3S histone deacetylase along the path of transcribing RNA polymerase II regulates access to DNA, contributing to faithful gene transcription. The association of Rpd3S with chromatin requires its Eaf3 subunit, which binds histone H3 methylated at lysine 36 (H3K36). Eaf3 is also part of NuA4 acetyltransferase that recognizes methylated H3K4. Here we show that Eaf3 in Saccharomyces cerevisiae contains a chromo barrel-related domain that binds methylated peptides, including H3K36 and H3K4, with low specificity and millimolar-range affinity. Nuclear magnetic resonance structure determination of Eaf3 bound to methylated H3K36 was accomplished by engineering a linked Eaf3-H3K36 molecule with a chemically incorporated methyllysine analog. Our study uncovers the molecular details of Eaf3-methylated H3K36 complex formation, and suggests that, in the cell, Eaf3 can only function within a framework of combinatorial interactions. This work also provides a general method for structure determination of low-affinity protein complexes implicated in methyllysine recognition. PubMed: 18818090DOI: 10.1016/j.str.2008.08.008 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
