1OZV

Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy

1OZV の概要

• エントリーDOI: 10.2210/pdb1ozv/pdb
• 関連するPDBエントリー: 1MLV
• 分子名称: Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplast, LYSINE, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• 機能のキーワード: set domain, lysine n-methylation, multiple methylation, photosynthesis, post-translational modification, transferase
• 由来する生物種: Pisum sativum (pea)
• 細胞内の位置: Plastid, chloroplast: Q43088
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 153482.30

構造登録者

Trievel, R.C.,Flynn, E.M.,Houtz, R.L.,Hurley, J.H. (登録日: 2003-04-09, 公開日: 2003-07-01, 最終更新日: 2023-08-16)

主引用文献

Trievel, R.C.,Flynn, E.M.,Houtz, R.L.,Hurley, J.H.
Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
Nat.Struct.Biol., 10:545-552, 2003

PubMed Abstract: SET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet) to specific lysine residues of protein substrates, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex. The crystal structures of pea Rubisco large subunit methyltransferase (LSMT) in ternary complexes with either lysine or epsilon-N-methyllysine (MeLys) and the product S-adenosylhomocysteine (AdoHcy) were determined to resolutions of 2.65 and 2.55 A, respectively. The zeta-methyl group of MeLys is bound to the enzyme via carbon-oxygen hydrogen bonds that play a key role in catalysis. The methyl donor and acceptor are aligned in a linear geometry for S(N)2 nucleophilic transfer of the methyl group during catalysis. Differences in hydrogen bonding between the MeLys epsilon-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys.

PubMed: 12819771
DOI: 10.1038/nsb946

実験手法

X-RAY DIFFRACTION (2.65 Å)