4O30

Crystal structure of ATXR5 in complex with histone H3.1 and AdoHcy

4O30 の概要

• エントリーDOI: 10.2210/pdb4o30/pdb
• 分子名称: Histone-lysine N-methyltransferase ATXR6, putative, histone H3.1, S-ADENOSYL-L-HOMOCYSTEINE, ... (6 entities in total)
• 機能のキーワード: histone methylation, chromatin, epigenetics, trithorax, set domain, lysine methyltransferases, pcna, histone h3, nucleus, transferase
• 由来する生物種: Ricinus communis (Castor bean); 詳細
• 細胞内の位置: Plastid, chloroplast (By similarity): B9RU15
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 58002.07

構造登録者

Bergamin, E.,Mongeon, V.,Couture, J.F. (登録日: 2013-12-17, 公開日: 2014-03-26, 最終更新日: 2024-02-28)

主引用文献

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

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: 24626927
DOI: 10.1126/science.1248357

実験手法

X-RAY DIFFRACTION (2.1 Å)