期刊
STRUCTURE
卷 10, 期 10, 页码 1303-1315出版社
CELL PRESS
DOI: 10.1016/S0969-2126(02)00852-3
关键词
knot; methyltransferase; S-adenosyl-L-methionine; SpoU family; 23S rRNA; ribosome maturation
In Escherichia coli, RImB 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 Angstrom resolution. RImB 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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