EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.1.297 | - |
Thermotoga maritima |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.1.1.297 | to 2.2 A resolution. The C-terminal domain of PrmC adopts the canonical S-adenosyl-L-methionine-dependent methyltransferase fold and shares structural similarity with the nucleotide N-methyltransferases in the active site, including use of a conserved (D/N)PPY motif to select and position the glutamine substrate. Residues of the PrmC 197NPPY200 motif form hydrogen bonds that position the planar Gln side chain such that the lone-pair electrons on the nitrogen nucleophile are oriented toward the methyl group of S-adenosyl-Lmethionine. In the product complex, the methyl group remains pointing toward the sulfur, consistent with either an sp3-hybridized, positively charged Gln nitrogen, or a neutral sp2-hybridized nitrogen in a strained conformation. Due to steric overlap within the active site, proton loss and formation of the neutral planar methylamide product are likely to occur during or after product release | Thermotoga maritima |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.297 | Thermotoga maritima | Q9WYV8 | - |
- |
2.1.1.297 | Thermotoga maritima DSM 3109 | Q9WYV8 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.297 | PrmC/HemK | - |
Thermotoga maritima |
2.1.1.297 | release factor glutamine methyltransferase | - |
Thermotoga maritima |