| DOI | Resolve DOI: https://doi.org/10.1016/S0969-2126(02)00852-3 |
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| Author | Search for: Michel, Gurvan1; Search for: Sauvé, Véronique1; Search for: Larocque, Robert1; Search for: Li, Yunge1; Search for: Matte, Allan1; Search for: Cygler, Miroslaw1 |
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| Affiliation | - National Research Council of Canada. NRC Biotechnology Research Institute
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| Format | Text, Article |
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| Subject | pharmaceutical; knot; methyltranferase; S-adenosyl-L-methionine; SpoU family; 23S rRNA; ribosome maturation |
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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 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. |
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| Publication date | 2002-10 |
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| In | |
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| Language | English |
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| NRC number | 44870 |
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| NPARC number | 3540078 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | f68bfc5e-d133-4883-9eb8-70c524cf6760 |
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| Record created | 2009-03-01 |
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| Record modified | 2020-03-30 |
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