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

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DOIResolve DOI: http://doi.org/10.1016/S0969-2126(02)00852-3
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TypeArticle
Journal titleStructure
Volume10
Issue10
Pages13031315; # of pages: 13
Subjectpha; knot; methyltranferase; S-adenosyl-L-methionine; SpoU family; 23S rRNA; ribosome maturation
AbstractIn 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
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number44870
NPARC number3540078
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Record identifierf68bfc5e-d133-4883-9eb8-70c524cf6760
Record created2009-03-01
Record modified2016-05-09
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