3FRH

Structure of the 16S rRNA methylase RmtB, P21

Summary for 3FRH

• Entry DOI: 10.2210/pdb3frh/pdb
• Related: 3FRI 3FZG
• Descriptor: 16S rRNA methylase, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• Functional Keywords: methyltransferase domain, helical n-terminal domain, methyltransferase, plasmid, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 28086.27

Authors

Schmitt, E.,Galimand, M.,Panvert, M.,Dupechez, M.,Courvalin, P.,Mechulam, Y. (deposition date: 2009-01-08, release date: 2009-08-11, Last modification date: 2023-11-01)

Primary citation

Schmitt, E.,Galimand, M.,Panvert, M.,Courvalin, P.,Mechulam, Y.
Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases
J.Mol.Biol., 388:570-582, 2009

PubMed Abstract: Aminoglycosides are used extensively for the treatment of severe infections due to Gram-negative bacteria. However, certain species have become highly resistant after acquisition of genes for methyltransferases which catalyze post-transcriptional methylation of N7-G1405 in 16 S rRNA of 30 S ribosomal subunits. Inactivation of this enzymatic activity is therefore an important challenge for development of an effective therapy. The present work describes the crystallographic structures of methyltransferases RmtB and ArmA from clinical isolates. Together with biochemical experiments, the 3D structures indicate that the N-terminal domain specific for this family of methyltransferases is required for enzymatic activity. Site-directed mutagenesis has enabled important residues for catalysis and RNA binding to be identified. These high-resolution structures should underpin the design of potential inhibitors of these enzymes, which could be used to restore the activity of aminoglycosides against resistant pathogens.

PubMed: 19303884
DOI: 10.1016/j.jmb.2009.03.034

Experimental method

X-RAY DIFFRACTION (1.2 Å)