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Literature summary for 6.1.1.2 extracted from
- Crystal structures of three protozoan homologs of tryptophanyl-tRNA synthetase (2011), Mol. Biochem. Parasitol., 177, 20-28.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the single TrpRS gene codes for an N-terminal domain of uncertain function in addition to the conserved core TrpRS domains | Cryptosporidium parvum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| active, truncated TrpRS lacking the N-terminal domain, sitting drop vapor diffusion at room temperature, 0.00015 ml of 24.7-32.1 mg/ml protein in 0.5 M NaCl, 25 mM HEPES, pH 7.5, 5% glycerol, and 0.025% Na-azide plus 10 mM ATP, 1 mM TCEP, 10 mM MgCl2, 2 mM L-tryptophan, is mixed with 0.00015 ml of reservoir solution containing 0.2 M MgCl2, 0.1 M Bis-Tris, pH 6.2, and 28% w/v PEG 3350, X-ray diffraction structure determination and analysis at 2.4 A resolution | Cryptosporidium parvum |
| cytosolic isoform, sitting drop vapor diffusion at room temperature, 0.0001 ml of 13.2 mg/ml protein in 0.5 M NaCl, 25 mM HEPES, pH 7.5, 5% glycerol, and 0.025% Na-azide is mixed with 0.0002 ml of reservoir solution containing 0.2 M Na-citrate, and 20% w/v PEG 3350, X-ray diffraction structure determination and analysis at 2.8 A resolution | Entamoeba histolytica |
| cytosolic isoform, sitting drop vapor diffusion at room temperature, 0.0001 ml of 17.8 mg/ml protein in 0.5 M NaCl, 25 mM HEPES, pH 7.5, 5% glycerol, and 0.025% Na-azide plus 1mM tris(2-carboxyethyl)phosphine is mixed with 0.0002 ml of reservoir solution containing 0.2 M Na malonate, pH 7.0, and 20% w/v PEG 3350. triclinic crystals X-ray diffraction structure determination and analysis at 2.8 A resolution | Trypanosoma brucei |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | Cryptosporidium parvum TrpRS remains fully active in charging tRNATrp after truncation of the N-terminal extra domain | Cryptosporidium parvum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Trypanosoma brucei | 5829 | - |
| cytosol | - |
Entamoeba histolytica | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Cryptosporidium parvum |  |
| Mg2+ | required | Trypanosoma brucei | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-tryptophan + tRNATrp | Cryptosporidium parvum | - |
AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | Trypanosoma brucei | - |
AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cryptosporidium parvum | Q5CYP8 | contains a single TrpRS gene | - |
| Entamoeba histolytica | C4LU94 | TrpRS homologue 1; the Entamoeba histolytica genome contains three sequences that appear to be TrpRS homologues | - |
| Entamoeba histolytica | C4LUB5 | TrpRS homologue 3; the Entamoeba histolytica genome contains three sequences that appear to be TrpRS homologues | - |
| Entamoeba histolytica | C4M7U9 | TrpRS homologue 2; the Entamoeba histolytica genome contains three sequences that appear to be TrpRS homologues | - |
| Trypanosoma brucei | Q580R7 | the Trypanosoma brucei genome contains separate cytosolic and mitochondrial isoforms of TrpRS that are both required and have diverged in their respective tRNA recognition domains | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-tryptophan + tRNATrp | - |
Cryptosporidium parvum | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | - |
Trypanosoma brucei | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | N-terminally truncated Cryptosporidium parvum TrpRS is able to charge Escherichia coli tRNATrp with 3H-labeled tryptophan. The N-terminal extension domain is not required for activity | Cryptosporidium parvum | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| ATP + L-tryptophan + tRNATrp | neither isoform is capable of charging recombinant Escherichia coli tRNATrp, they are specific for trypanosomal tRNATrp | Trypanosoma brucei | AMP + diphosphate + L-tryptophyl-tRNATrp | - |
? | |
| additional information | the homologue with defective active site is not capable of charging tRNA | Entamoeba histolytica | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | amino acid sequence and structure comparisons of Entamoeba histolytica, Trypanosoma brucei, and Cryptosporidium parvum, overview | Cryptosporidium parvum |
| More | amino acid sequence and structure comparisons of Entamoeba histolytica, Trypanosoma brucei, and Cryptosporidium parvum, overview | Trypanosoma brucei |
| More | amino acid sequence and structure comparisons of Entamoeba histolytica, Trypanosoma brucei, and Cryptosporidium parvum, overview | Entamoeba histolytica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS | Cryptosporidium parvum |
| More | TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS | Trypanosoma brucei |
| More | TrpRS is a class I aminoacyl-tRNA synthetase characterized by a Rossmann-fold catalytic domain whose active site is recognizable by the presence of two conserved sequence motifs with consensus sequences HIGH and KMSKS | Entamoeba histolytica |
| TrpRS | - |
Cryptosporidium parvum |
| TrpRS | - |
Trypanosoma brucei |
| TrpRS | - |
Entamoeba histolytica |
| Tryptophanyl-tRNA synthetase | - |
Cryptosporidium parvum |
| Tryptophanyl-tRNA synthetase | - |
Trypanosoma brucei |
| Tryptophanyl-tRNA synthetase | - |
Entamoeba histolytica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Cryptosporidium parvum |
| 22 | - |
assay at room temperature | Trypanosoma brucei |
| 22 | - |
assay at room temperature | Entamoeba histolytica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Cryptosporidium parvum |
| 7 | - |
assay at | Trypanosoma brucei |
| 7 | - |
assay at | Entamoeba histolytica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Trypanosoma brucei | |
| ATP | ATP-binding motif KMSAS | Cryptosporidium parvum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the Trypanosoma brucei genome contains separate cytosolic and mitochondrial isoforms of TrpRS that are both required and have diverged in their respective tRNA recognition domains | Trypanosoma brucei |
| additional information | one of the TrpRS gene homologues has lost the active site motifs characteristic of the class I aminoacyl-tRNA synthetase catalytic domain while retaining the conserved features of a fully formed tRNATrp recognition domain | Entamoeba histolytica |
| physiological function | the organism requires a separate mitochondrial TrpRS isoform because the majority of tRNATrp in the trypanosomatid mitochondrion is posttranscriptionally modified by thiolation of U33 and by RNA-editing of the anticodon, residues 34-36, from CCA to UCA | Trypanosoma brucei |
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Release 2023.1 (January 2023)
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