The structure of the RlmB 23S rRNA Methyltransferase reveals a new Methyltransferase fold with a unique knot

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1016/S0969-2126(02)00852-3
AuthorSearch for: 1 ; Search for: 1 ; Search for: 1 ; Search for: 1 ; Search for: 1 ; Search for: 1 
Name affiliation
  1. National Research Council Canada. NRC Biotechnology Research Institute
FormatText
TypeArticle
Journal titleStructure
Volume10
Issue10
Pages1303–1315; # of pages: 13
Subjectpha; knot; methyltranferase; S-adenosyl-L-methionine; SpoU family; 23S rRNA; ribosome maturation
Abstract
In Escherichia coli, RlmB catalyzes the methylation of guanosine 2251, a modification conserved in the peptidyltransferase domain of 23S rRNA. The crystal structure of this 2′O-methyltransferase has been determined at 2.5 Å resolution. RlmB consists of an N-terminal domain connected by a flexible extended linker to a catalytic C-terminal domain and forms a dimer in solution. The C-terminal domain displays a divergent methyltransferase fold with a unique knotted region, and lacks the classic AdoMet binding site features. The N-terminal domain is similar to ribosomal proteins L7 and L30, suggesting a role in 23S rRNA recognition. The conserved residues in this novel family of 2′O-methyltransferases cluster in the knotted region, suggesting the location of the catalytic and AdoMet binding sites.
Publication date
LanguageEnglish
NRC number44870
NPARC number3540078
Export citationExport as RIS
Report a correctionReport a correction
Record identifierf68bfc5e-d133-4883-9eb8-70c524cf6760
Record created2009-03-01
Record modified2019-02-18
Date modified:
Report a problem on this page