2RSD

Solution structure of the plant homeodomain (PHD) of the E3 SUMO ligase Siz1 from rice

2RSD の概要

• エントリーDOI: 10.2210/pdb2rsd/pdb
• NMR情報: BMRB: 11469
• 分子名称: E3 SUMO-protein ligase SIZ1, ZINC ION (2 entities in total)
• 機能のキーワード: e3 sumo ligase, plant homeodomain (phd), histone binding, ligase
• 由来する生物種: Oryza sativa Japonica Group (Japanese rice)
• 細胞内の位置: Nucleus (By similarity): Q6L4L4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7802.54

構造登録者

Shindo, H.,Tsuchiya, W.,Suzuki, R.,Yamazaki, T. (登録日: 2012-01-12, 公開日: 2012-08-15, 最終更新日: 2024-05-15)

主引用文献

Shindo, H.,Suzuki, R.,Tsuchiya, W.,Taichi, M.,Nishiuchi, Y.,Yamazaki, T.
PHD finger of the SUMO ligase Siz/PIAS family in rice reveals specific binding for methylated histone H3 at lysine 4 and arginine 2
Febs Lett., 586:1783-1789, 2012

PubMed Abstract: We determined the three-dimensional structure of the PHD finger of the rice Siz/PIAS-type SUMO ligase, OsSiz1, by NMR spectroscopy and investigated binding ability for a variety of methylated histone H3 tails, showing that OsSiz1-PHD primarily recognizes dimethylated Arg2 of the histone H3 and that methylations at Arg2 and Lys4 reveal synergy effect on binding to OsSiz1-PHD. The K4 cage of OsSiz1-PHD for trimethylated Lys4 of H3K4me3 was similar to that of the BPTF-PHD finger, while the R2 pocket for Arg2 was different. It is intriguing that the PHD module of Siz/PIAS plays an important role, with collaboration with the DNA binding domain SAP, in gene regulation through SUMOylation of a variety of effectors associated with the methylated arginine-riched chromatin domains.

PubMed: 22626555
DOI: 10.1016/j.febslet.2012.04.063

実験手法

SOLUTION NMR