PMID:12377117
| Citation |
Michel, G, Sauvé, V, Larocque, R, Li, Y, Matte, A and Cygler, M (2002) The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot. Structure 10:1303-15 |
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| 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 A 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. |
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| Keywords |
Amino Acid Sequence; Catalytic Domain; Dimerization; Escherichia coli/enzymology; Methyltransferases/chemistry; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Folding; RNA, Ribosomal, 23S/chemistry; Sequence Homology, Amino Acid |
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