EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.1.1.11 | crystal structures of the SerRS from the archaeon Pyrococcus horikoshii bound with 5'-O-[N-(L-seryl)-sulfamoyl]-adenosine are solved at 2.6 A, with ATP at 2.8 A, and in the apo form at 3.0 A. SerRS recognizes the seryl and adenylate moieties in a manner similar to those of the bacterial and mitochondrial SerRSs from Thermus thermophilus and Bos taurus, respectively, but different from that of the unusual SerRS from the methanogenic archaeon Methanosarcina barkeri | Pyrococcus horikoshii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.1.1.11 | additional information | models of Pyrococcus horikoshii SerRS bound with the Thermus thermophilus and Pyrococcus horikoshii tRNA(Ser)s suggest that the helical domain of Pyrococcus horikoshii SerRS is involved in the extra arm binding. This region of SerRS has additional basic residues as compared with Thermus thermophilus SerRS, and a Trp residue specific to the archaeal/eukaryal SerRSs. Mutational analyses reveales that the basic and Trp residues are important for tRNA aminoacylation | Pyrococcus horikoshii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.11 | Pyrococcus horikoshii | O58441 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.11 | ATP + L-serine + tRNASer | SerRS efficiently aminoacylates not only Pyrococcus horikoshii tRNA(Ser) but also bacterial tRNA(Ser)s from Thermus thermophilus and Escherichia coli | Pyrococcus horikoshii | AMP + diphosphate + L-seryl-tRNASer | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.11 | SerRS | - |
Pyrococcus horikoshii |
6.1.1.11 | Seryl-tRNA synthetase | - |
Pyrococcus horikoshii |