3CJR

Ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11 (K39A) and inhibitor Sinefungin.

3CJR の概要

• エントリーDOI: 10.2210/pdb3cjr/pdb
• 関連するPDBエントリー: 1UFK 2NXC 2NXE 2NXJ 2NXN 3CJQ 3CJS 3CJT 3CJU
• 分子名称: Ribosomal protein L11 methyltransferase, 50S ribosomal protein L11, SINEFUNGIN, ... (4 entities in total)
• 機能のキーワード: s-adenosyl-l-methionine dependent methyltransferase, post-translational modification, multi-specific trimethylation, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, transferase-ribosomal protein complex, transferase/ribosomal protein
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q84BQ9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43511.20

構造登録者

Demirci, H.,Gregory, S.T.,Dahlberg, A.E.,Jogl, G. (登録日: 2008-03-13, 公開日: 2008-05-20, 最終更新日: 2023-08-30)

主引用文献

Demirci, H.,Gregory, S.T.,Dahlberg, A.E.,Jogl, G.
Multiple-Site Trimethylation of Ribosomal Protein L11 by the PrmA Methyltransferase.
Structure, 16:1059-1066, 2008

PubMed Abstract: Ribosomal protein L11 is a universally conserved component of the large subunit, and plays a significant role during initiation, elongation, and termination of protein synthesis. In Escherichia coli, the lysine methyltransferase PrmA trimethylates the N-terminal alpha-amino group and the epsilon-amino groups of Lys3 and Lys39. Here, we report four PrmA-L11 complex structures in different orientations with respect to the PrmA active site. Two structures capture the L11 N-terminal alpha-amino group in the active site in a trimethylated post-catalytic state and in a dimethylated state with bound S-adenosyl-L-homocysteine. Two other structures show L11 in a catalytic orientation to modify Lys39 and in a noncatalytic orientation. The comparison of complex structures in different orientations with a minimal substrate recognition complex shows that the binding mode remains conserved in all L11 orientations, and that substrate orientation is brought about by the unusual interdomain flexibility of PrmA.

PubMed: 18611379
DOI: 10.1016/j.str.2008.03.016

実験手法

X-RAY DIFFRACTION (2.05 Å)