Data extracted from this reference:
Cloned(Commentary)
Engineering
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
Reaction
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)
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
710548
Escherichia coli
adenylated TPHE39A + diphosphate
?
Cloned(Commentary) (protein specific)
Engineering (protein specific)
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
Substrates and Products (Substrate) (protein specific)
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
710548
Escherichia coli
adenylated TPHE39A + diphosphate
?
Other publictions for EC 2.7.7.B5
725262
Martinez-Gomez
The rhodanese domain of ThiI i ...
Salmonella enterica
J. Bacteriol.
193
4582-4587
2011
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710548
Tanaka
Deduced RNA binding mechanism ...
Escherichia coli
RNA
15
1498-1506
2009
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691789
You
Direct evidence that thil is a ...
Escherichia coli
ChemBioChem
9
1879-1882
2008
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694560
Naumann
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Versuche zur Strukturaufkläru ...
Escherichia coli, Thermotoga maritima
PH. D. Thesis Universität Göttingen
2005
0000
2005
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