EC Number   |
Reference |
|---|
   6.3.4.19 | crystal structure of Aquifex aeolicus TilS, complexed with ATP, Mg2+, and L-lysine, at 2.5 A resolution. The presence of the TilS-specific subdomain causes the active site to have two separate gateways, a large hole and a narrow tunnel on the opposite side. ATP is bound inside the hole, and L-lysine is bound at the entrance of the tunnel. The conserved Asp36 in the PP-motif coordinates Mg2+. In these initial binding modes, the ATP, Mg2+, and L-lysine are held far apart from each other, but they seem to be brought together for the reaction upon cytidine binding, with putative structural changes of the complex |
706782 |
| 6.3.4.19 | crystal structure of Geobacillus kaustophilus TilS complexed with Bacillus subtilis tRNAIle CAU at 3.65 A resolution, by the multiwavelength anomalous dispersion method. The asymmetric unit contains one TilS homodimer and two tRNAs, each tightly embedded in one monomer of TilS, with an overall interface of 2998 A. Each monomer consists of an amino-terminal catalytic domain, and two carboxy-terminal domains, connected by a long a-helical linker and a loop linker, respectively |
705888 |
| 6.3.4.19 | crystal structure of TilS at 2.42 A resolution. Structural and functional comparisons with Escherichia coli TilS reveals that the two TilS enzymes discriminate premodified tRNAIle2 from premodified tRNAMet by strategies similar to that used by IleRS, but in distinct manners |
706481 |
| 6.3.4.19 | structural and functional comparisons of Escherichia coli TilS and Axifex aeolicus TilS reveal that the two TilS enzymes discriminate premodified tRNAIle2 from premodified tRNAMet bystrategies similar to that used by IleRS, but in distinct manners |
706481 |
