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Literature summary for 2.7.7.B5 extracted from

  • Tanaka, Y.; Yamagata, S.; Kitago, Y.; Yamada, Y.; Chimnaronk, S.; Yao, M.; Tanaka, I.
    Deduced RNA binding mechanism of ThiI based on structural and binding analyses of a minimal RNA ligand (2009), RNA, 15, 1498-1506.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of two truncated forms of ThiI containing the N-terminal domain including NFLD and THUMP, and the C-terminal domain including the PP-loop and RLD domains, respectively. The N-domain can bind with both tRNAPhe and TPHE39A and recognizes the acceptor-stem region, whereas the C-domain cannot. The C-domain also affects RNA binding by its enthalpically favorable, but entropically unfavorable, contribution. The C-domain induces a conformation change in tRNAPhe Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Reaction

Reaction Comment Organism Reaction ID
tRNA-uridine + ATP = adenylated-trNA-uridine + diphosphate RNA binding mechanism of ThiI in which the N-terminal domain recognizes the acceptor-stem region and the C-terminal region causes a conformational change of RNA Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + TPHE39A truncated tRNA consisting of 39 nucleotides derived from tRNAPhe, minimal RNA substrate for modification by ThiI. The crystal structure of TPHE39A shows that base pairs in the T-stem are almost completely disrupted, although those in the acceptor-stem are preserved. ThiI can efficiently bind with not only tRNAPhe but also TPHE39A Escherichia coli adenylated TPHE39A + diphosphate
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