Cloned (Comment) | Organism |
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- |
Escherichia coli |
Protein Variants | Comment | Organism |
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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 | UniProt | Comment | Textmining |
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Escherichia coli | - |
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Reaction | Comment | Organism | Reaction ID |
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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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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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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