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show all sequences of 2.7.7.B5

Deduced RNA binding mechanism of ThiI based on structural and binding analyses of a minimal RNA ligand

Tanaka, Y.; Yamagata, S.; Kitago, Y.; Yamada, Y.; Chimnaronk, S.; Yao, M.; Tanaka, I.; RNA 15, 1498-1506 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Escherichia coli
Engineering
Amino acid exchange
Commentary
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
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Reaction
Reaction
Commentary
Organism
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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)
Commentary
Organism
-
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
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
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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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