EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.1.186 | gene rlmM, expression of His-tagged RlmM in Escherichia coli strain BL21(DE3) | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.1.1.186 | purified recombinant His-tagged RlmM free or in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, 0.0015 ml 10 mg/ml protein solution os mixed with 0.0015 ml of reservoir solution containing 0.3 M ammonium tartrate, pH 7.0, and 20% PEG 3350, 20°C, 1 week, two crystal forms, X-ray diffraction structure determination and analysis at 1.9 A and 2.6 A resolution, respectively, molecular replacement | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.186 | Mg2+ | required | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.186 | S-adenosyl-L-methionine + cytidine2498 in 23S rRNA | Escherichia coli | RlmM is active on 23S rRNA from an RlmM knockout strain but not on mature 50S subunits from the same strain | S-adenosyl-L-homocysteine + 2'-O-methylcytidine2498 in 23S rRNA | - |
? | |
2.1.1.186 | S-adenosyl-L-methionine + cytidine2498 in 23S rRNA | Escherichia coli BW25113 | RlmM is active on 23S rRNA from an RlmM knockout strain but not on mature 50S subunits from the same strain | S-adenosyl-L-homocysteine + 2'-O-methylcytidine2498 in 23S rRNA | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.186 | Escherichia coli | P0ADR6 | gene rlmM | - |
2.1.1.186 | Escherichia coli BW25113 | P0ADR6 | gene rlmM | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.1.186 | recombinant His-tagged RlmM from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.186 | S-adenosyl-L-methionine + cytidine2498 in 23S rRNA | RlmM is active on 23S rRNA from an RlmM knockout strain but not on mature 50S subunits from the same strain | Escherichia coli | S-adenosyl-L-homocysteine + 2'-O-methylcytidine2498 in 23S rRNA | - |
? | |
2.1.1.186 | S-adenosyl-L-methionine + cytidine2498 in 23S rRNA | 23S rRNA substrate structure, overview. The S-adenosyl-L-methionine-binding site is open and shallow, suggesting that RNA substrate binding may be required to form a conformation needed for catalysis. RlmM uses one side of the two domains and the inter-domain linker to recognize its RNA substrate | Escherichia coli | S-adenosyl-L-homocysteine + 2'-O-methylcytidine2498 in 23S rRNA | - |
? | |
2.1.1.186 | S-adenosyl-L-methionine + cytidine2498 in 23S rRNA | RlmM is active on 23S rRNA from an RlmM knockout strain but not on mature 50S subunits from the same strain | Escherichia coli BW25113 | S-adenosyl-L-homocysteine + 2'-O-methylcytidine2498 in 23S rRNA | - |
? | |
2.1.1.186 | S-adenosyl-L-methionine + cytidine2498 in 23S rRNA | 23S rRNA substrate structure, overview. The S-adenosyl-L-methionine-binding site is open and shallow, suggesting that RNA substrate binding may be required to form a conformation needed for catalysis. RlmM uses one side of the two domains and the inter-domain linker to recognize its RNA substrate | Escherichia coli BW25113 | S-adenosyl-L-homocysteine + 2'-O-methylcytidine2498 in 23S rRNA | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.1.186 | More | RlmM consists of an N-terminal THUMP domain and a C-terminal catalytic Rossmann-like fold MTase domain in a distinct arrangement, detailed structure analysis, overview | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.186 | 2O-ribose methyltransferase | - |
Escherichia coli |
2.1.1.186 | RlmM | - |
Escherichia coli |
2.1.1.186 | ygdE | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.1.186 | 37 | - |
assay at | Escherichia coli |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.1.186 | additional information | - |
Na2SO4 gives the highest thermal stability to RlmM | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.1.1.186 | 7.6 | - |
assay at | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.186 | S-adenosyl-L-methionine | the S-adenosyl-L-methionine-binding site is open and shallow | Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.1.1.186 | evolution | the catalytic domain of RlmM is closely related to YiiB, TlyA and fibrillarins, with the second K of the catalytic tetrad KDKE shifted by two residues at the C-terminal end of a beta strand compared with most 2'O MTases | Escherichia coli |
2.1.1.186 | physiological function | RlmM catalyzes the S-adenosyl methionine-dependent 20O methylation of C2498 in 23S ribosomal RNA of Escherichia coli | Escherichia coli |