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Literature summary for 6.1.1.17 extracted from

  • Chongdar, N.; Dasgupta, S.; Datta, A.B.; Basu, G.
    Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase (2015), Biosci. Rep., 35, e00184 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.17

Cloned(Commentary)

Cloned (Comment) Organism
gene GluS, DNA and amino acid sequence determination and analysis Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information generation of pZBD-chimeras of Ec-GluRS, four chimeric versions with partly replaced zinc-binding motif, pZBD. In the first chimera [Ec(Te)-GluRS], the pZBD of Ec-GluRS is replaced by the corresponding pZBD from Thermosynechococcus elongatus GluRS (Te-GluRS) whose structure is devoid of a bound Zn2+ despite containing the modified ZB-motif CxCxnYx3H. In the second chimera [Ec(EQRS)-GluRS] the pZBD of Ec-GluRS is replaced by the corresponding pZBD from Escherichia coli Glu-QRS (Ec-EQRS) whose zinc-bound structure contains the ZB-motif CxCxnYx3C. In the third chimera [Ec(Bt)-GluRS], the pZBD of Ec-GluRS is replaced by a 19-residue stretch from the pZBD of Bt-GluRS which contains a disrupted zinc binding motif CxMx20Yx3W and whose structure is devoid of a bound Zn2+ ion. The 19-residue stretch starts from the residue preceding the fourth zinc-co-ordinating cysteine residue in Ec-GluRS and continues until the last beta-strand of the pZBD fold. The overall secondary structure and compactness of wild-type Ec-GluRS remains unaltered in the chimeric constructs. The association of GluRS with tRNAGlu but not with ATP is sensitive to pZBD perturbations. Except for Ec(Bt)-GluRS, all pZBD-chimeras show 100fold or more reduced catalytic efficiency and contain zinc. Natively zinc-bound Ec-GluRS does not require zinc to be active Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Zn2+ dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase, overview. The association of enzyme GluRS with tRNAGlu but not with ATP is sensitive to perturbations of the zinc binding domain. Natively zinc-bound Ec-GluRS does not require zinc to be active Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate + tRNAGlu Escherichia coli
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P04805
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate + tRNAGlu
-
 Escherichia coli AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
additional information efficient glutamylation demands optimal binding of substrates (ATP, tRNAGlu and L-glutamic acid) by GluRS. Binding of tRNAGlu induces conformational changes in GluRS that stimulates the binding of L-glutamic acid leading to the productive binding of ATP. L-glutamic acid is first activated by GluRS in presence of ATP to form the adenylate complex. This is followed by the catalytic step where the acceptor stem of tRNAGlu is glutamylated Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
Ec-GluRS
-
 Escherichia coli
GluRS
-
 Escherichia coli
Glutamyl-tRNA synthetase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli