The Structure of the RlmB 23S rRNA Methyltransferase Reveals a New Methyltransferase Fold with a Unique Knot

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 ex...

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Bibliographic Details
Published in:Structure (London) 2002-10, Vol.10 (10), p.1303-1315
Main Authors: Michel, Gurvan, Sauvé, Véronique, Larocque, Robert, Li, Yunge, Matte, Allan, Cygler, Miroslaw
Format: Article
Language:English
Subjects:
23S rRNA
Amino Acid Sequence
BASIC BIOLOGICAL SCIENCES
BIOCHEMISTRY
BNL
Catalytic Domain
Dimerization
Escherichia coli - enzymology
knot
METHYL TRANSFERASES
methyltransferase
Methyltransferases - chemistry
Models, Molecular
Molecular Sequence Data
national synchrotron light source
Protein Conformation
Protein Folding
ribosome maturation
RNA, Ribosomal, 23S - chemistry
S-adenosyl-L-methionine
Sequence Homology, Amino Acid
SpoU family
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Summary: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.
ISSN:0969-2126
0021-9258
1878-4186
1083-351X
DOI:10.1016/S0969-2126(02)00852-3