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