4O30
Crystal structure of ATXR5 in complex with histone H3.1 and AdoHcy
Summary for 4O30
| Entry DOI | 10.2210/pdb4o30/pdb |
| Descriptor | Histone-lysine N-methyltransferase ATXR6, putative, histone H3.1, S-ADENOSYL-L-HOMOCYSTEINE, ... (6 entities in total) |
| Functional Keywords | histone methylation, chromatin, epigenetics, trithorax, set domain, lysine methyltransferases, pcna, histone h3, nucleus, transferase |
| Biological source | Ricinus communis (Castor bean) More |
| Cellular location | Plastid, chloroplast (By similarity): B9RU15 |
| Total number of polymer chains | 4 |
| Total formula weight | 58002.07 |
| Authors | Bergamin, E.,Mongeon, V.,Couture, J.F. (deposition date: 2013-12-17, release date: 2014-03-26, Last modification date: 2024-02-28) |
| Primary citation | Jacob, Y.,Bergamin, E.,Donoghue, M.T.,Mongeon, V.,LeBlanc, C.,Voigt, P.,Underwood, C.J.,Brunzelle, J.S.,Michaels, S.D.,Reinberg, D.,Couture, J.F.,Martienssen, R.A. Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication. Science, 343:1249-1253, 2014 Cited by PubMed Abstract: Histone variants have been proposed to act as determinants for posttranslational modifications with widespread regulatory functions. We identify a histone-modifying enzyme that selectively methylates the replication-dependent histone H3 variant H3.1. The crystal structure of the SET domain of the histone H3 lysine-27 (H3K27) methyltransferase ARABIDOPSIS TRITHORAX-RELATED PROTEIN 5 (ATXR5) in complex with a H3.1 peptide shows that ATXR5 contains a bipartite catalytic domain that specifically "reads" alanine-31 of H3.1. Variation at position 31 between H3.1 and replication-independent H3.3 is conserved in plants and animals, and threonine-31 in H3.3 is responsible for inhibiting the activity of ATXR5 and its paralog, ATXR6. Our results suggest a simple model for the mitotic inheritance of the heterochromatic mark H3K27me1 and the protection of H3.3-enriched genes against heterochromatization during DNA replication. PubMed: 24626927DOI: 10.1126/science.1248357 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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