5O96

Structure of the putative methyltransferase Lpg2936 from Legionella pneumophila in complex with the bound cofactor SAM

Summary for 5O96

• Entry DOI: 10.2210/pdb5o96/pdb
• Descriptor: Ribosomal RNA small subunit methyltransferase E, S-ADENOSYLMETHIONINE (3 entities in total)
• Functional Keywords: rna methyltransferase, rsme-like, sam, s-adenosylmethionine, transferase
• Biological source: Legionella pneumophila
• Cellular location: Cytoplasm : Q5ZRE6
• Total number of polymer chains: 8
• Total formula weight: 221945.42

Authors

Pinotsis, N.,Waksman, G. (deposition date: 2017-06-15, release date: 2017-11-08, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)