2LXE

S4wyild

2LXE の概要

• エントリーDOI: 10.2210/pdb2lxe/pdb
• NMR情報: BMRB: 18672
• 分子名称: Histone-lysine N-methyltransferase SUVR4 (1 entity in total)
• 機能のキーワード: ubiqutine binding domain, a-helical, transferase
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12164.61

構造登録者

Kristiansen, P.,Rahman, M.A.,Aalen, R.B. (登録日: 2012-08-20, 公開日: 2013-11-20, 最終更新日: 2024-05-15)

主引用文献

Rahman, M.A.,Kristiansen, P.E.,Veiseth, S.V.,Andersen, J.T.,Yap, K.L.,Zhou, M.M.,Sandlie, I.,Thorstensen, T.,Aalen, R.B.
The arabidopsis histone methyltransferase SUVR4 binds ubiquitin via a domain with a four-helix bundle structure.
Biochemistry, 53:2091-2100, 2014

PubMed Abstract: In eukaryotes, different chromatin states facilitate or repress gene expression and restrict the activity of transposable elements. Post-translational modifications (PTMs) of amino acid residues on the N-terminal tails of histones are suggested to define such states. The histone lysine methyltransferase (HKMTase) SU(VAR)3-9 RELATED4 (SUVR4) of Arabidopsis thaliana functions as a repressor of transposon activity. Binding of ubiquitin by the WIYLD domain facilitates the addition of two methyl groups to monomethylated lysine 9 of histone H3. By using nuclear magnetic resonance (NMR) spectroscopy, we identified SUVR4 WIYLD (S4WIYLD) as a domain with a four-helix bundle structure, in contrast to three-helix bundles of other ubiquitin binding domains. NMR titration analyses showed that residues of helix α1 (Q38, L39, and D40) and helix α4 (N68, T70, A71, V73, D74, I76, S78, and E82) of S4WIYLD and residues between the first and second β-strands (T9 and G10) and on β-strands 3 (R42, G47, K48, and Q49) and 4 (H68, R72, and L73) undergo significant chemical shift changes when the two proteins interact. A model of the complex, generated using HADDOCK, suggests that the N-terminal and C-terminal parts of S4WIYLD constitute a surface that interacts with charged residues close to the hydrophobic patch of ubiquitin. The WIYLD domains of the closely related SUVR1 and SUVR2 Arabidopsis proteins also bind ubiquitin, indicating that this is a general feature of this domain. The question of whether SUVR proteins act as both readers of monoubiquitinated H2B and writers of histone PTMs is discussed.

PubMed: 24625295
DOI: 10.1021/bi401436h

実験手法

SOLUTION NMR