2R3A
Methyltransferase domain of human suppressor of variegation 3-9 homolog 2
Summary for 2R3A
| Entry DOI | 10.2210/pdb2r3a/pdb |
| Descriptor | Histone-lysine N-methyltransferase SUV39H2, ZINC ION, S-ADENOSYLMETHIONINE, ... (5 entities in total) |
| Functional Keywords | histone h3-k9 methyltransferase 2, histone-lysine n-methyltransferase, h3 lysine-9 specific 2, alternative splicing, cell cycle, chromatin regulator, chromosomal protein, differentiation, nucleus, repressor, s-adenosyl-l-methionine, telomere, transcription, transcription regulation, structural genomics, structural genomics consortium, sgc, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus (By similarity): Q9H5I1 |
| Total number of polymer chains | 1 |
| Total formula weight | 34745.71 |
| Authors | Lunin, V.V.,Wu, H.,Zeng, H.,Ren, H.,Loppnau, P.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Plotnikov, A.N.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2007-08-29, release date: 2007-09-11, Last modification date: 2023-08-30) |
| Primary citation | Wu, H.,Min, J.,Lunin, V.V.,Antoshenko, T.,Dombrovski, L.,Zeng, H.,Allali-Hassani, A.,Campagna-Slater, V.,Vedadi, M.,Arrowsmith, C.H.,Plotnikov, A.N.,Schapira, M. Structural biology of human H3K9 methyltransferases Plos One, 5:e8570-e8570, 2010 Cited by PubMed Abstract: SET domain methyltransferases deposit methyl marks on specific histone tail lysine residues and play a major role in epigenetic regulation of gene transcription. We solved the structures of the catalytic domains of GLP, G9a, Suv39H2 and PRDM2, four of the eight known human H3K9 methyltransferases in their apo conformation or in complex with the methyl donating cofactor, and peptide substrates. We analyzed the structural determinants for methylation state specificity, and designed a G9a mutant able to tri-methylate H3K9. We show that the I-SET domain acts as a rigid docking platform, while induced-fit of the Post-SET domain is necessary to achieve a catalytically competent conformation. We also propose a model where long-range electrostatics bring enzyme and histone substrate together, while the presence of an arginine upstream of the target lysine is critical for binding and specificity. PubMed: 20084102DOI: 10.1371/journal.pone.0008570 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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