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Literature summary for 6.1.1.6 extracted from

  • Sakurama, H.; Takita, T.; Mikami, B.; Itoh, T.; Yasukawa, K.; Inouye, K.
    Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate (2009), J. Biochem., 145, 555-563.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of two complexes of LysRS with the adenylate of L-lysine hydroxamate and with 5'-O-[N-(L-Lysyl)sulphamoyl] adenosine. The comparisons of the two structures and the SerRS structure reveals the specific side-chain shift of Glu411 of LysRS in the complex with the adenylate of L-lysine hydroxamate. Glu411 plays a key role in the arrangement of diphosphate for the nucleophilic attack Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus Q9RHV9
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Reaction

Reaction Comment Organism Reaction ID
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys residue Glu411 plays a key role in the arrangement of diphosphate for the nucleophilic attack Geobacillus stearothermophilus