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Literature summary for 6.3.4.19 extracted from

  • Kuratani, M.; Yoshikawa, Y.; Bessho, Y.; Higashijima, K.; Ishii, T.; Shibata, R.; Takahashi, S.; Yutani, K.; Yokoyama, S.
    Structural basis of the initial binding of tRNA(Ile) lysidine synthetase TilS with ATP and L-lysine (2007), Structure, 15, 1642-1653.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Aquifex aeolicus O67728
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[tRNAIle2]-cytidine34 + L-lysine + ATP
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Aquifex aeolicus [tRNAIle2]-2-L-lysylcytidine34 + AMP + diphosphate
-
?

Synonyms

Synonyms Comment Organism
TilS
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Aquifex aeolicus