Crystallization (Comment) | Organism |
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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 | Aquifex aeolicus |
Organism | UniProt | Comment | Textmining |
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Aquifex aeolicus | O67728 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
[tRNAIle2]-cytidine34 + L-lysine + ATP | - |
Aquifex aeolicus | [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate | - |
? |
Synonyms | Comment | Organism |
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TilS | - |
Aquifex aeolicus |