5O95

Structure of the putative methyltransferase Lpg2936 from Legionella pneumophila

5O95 の概要

• エントリーDOI: 10.2210/pdb5o95/pdb
• 分子名称: Ribosomal RNA small subunit methyltransferase E (2 entities in total)
• 機能のキーワード: rna methyltransferase, rsme-like, transferase
• 由来する生物種: Legionella pneumophila
• 細胞内の位置: Cytoplasm : Q5ZRE6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 109378.96

構造登録者

Pinotsis, N.,Waksman, G. (登録日: 2017-06-15, 公開日: 2017-11-08, 最終更新日: 2024-01-17)

主引用文献

Pinotsis, N.,Waksman, G.
Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S-adenosyl-L-methionine reveals novel insights into the mechanism of RsmE family methyltransferases.
Protein Sci., 26:2381-2391, 2017

PubMed Abstract: The methylation of U1498 located in the 16S ribosomal RNA of Escherichia coli is an important modification affecting ribosomal activity. RsmE methyltransferases methylate specifically this position in a mechanism that requires an S-adenosyl-L-methionine (AdoMet) molecule as cofactor. Here we report the structure of Apo and AdoMet-bound Lpg2936 from Legionella pneumophila at 1.5 and 2.3 Å, respectively. The protein comprises an N-terminal PUA domain and a C-terminal SPOUT domain. The latter is responsible for protein dimerization and cofactor binding. Comparison with similar structures suggests that Lpg2936 is an RsmE-like enzyme that can target the equivalent of U1498 in the L. pneumophila ribosomal RNA, thereby potentially enhancing ribosomal activity during infection-mediated effector production. The multiple copies of the enzyme found in both structures reveal a flexible conformation of the bound AdoMet ligand. Isothermal titration calorimetry measurements suggest an asymmetric two site binding mode. Our results therefore also provide unprecedented insights into AdoMet/RsmE interaction, furthering our understanding of the RsmE catalytic mechanism.

PubMed: 28940762
DOI: 10.1002/pro.3305

実験手法

X-RAY DIFFRACTION (1.491 Å)