Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Thermus thermophilus |
Crystallization (Comment) | Organism |
---|---|
structure of the TtuA-TtuB complex, at a resolution of 2.5 A, showing the S transfer of TtuB to tRNA using its C-terminal thiocarboxylate group. The active site of TtuA is connected to the outside by two channels, one occupied by TtuB and the other used for tRNA binding | Thermus thermophilus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | 3.84 mol per mol of enzyme | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O | Thermus thermophilus | - |
AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly | - |
? | |
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O | Thermus thermophilus DSM 7039 | - |
AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q72LF3 | - |
- |
Thermus thermophilus DSM 7039 | Q72LF3 | - |
- |
Oxidation Stability | Organism |
---|---|
TtuA is an oxygen-labile iron-sulfur protein | Thermus thermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O | - |
Thermus thermophilus | AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly | - |
? | |
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O | - |
Thermus thermophilus DSM 7039 | AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
[4Fe-4S]-center | TtuA requires oxygen-labile [4Fe-4S]-type iron (Fe)-S clusters for its enzymatic activity. The [4Fe-4S] cluster is coordinated by three highly conserved cysteine residues, and one of the Fe atoms is exposed to the active site. The cluster is coordinated by conserved residues Cys130, Cys133, and Cys222 | Thermus thermophilus |