Cloned (Comment) | Organism |
---|---|
gene structure and motifs in double-length TyrRS homologues, phylogenetic comparison | Leishmania major |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
fisetin | binding structure, overview | Leishmania major | |
tyrosinol | binding structure, overview | Leishmania major |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leishmania major | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | two distinct conformational states of the active site in the three Leishmania major TyrRS structures | Leishmania major | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the single tyrosyl-tRNA synthetase gene in trypanosomatid genomes codes for a protein that is twice the length of TyrRS from virtually all other organisms. Each half of the double-length TyrRS contains a catalytic domain and an anticodon-binding domain. Leishmania major TyrRS shows, that the two halves of a single molecule form a pseudo-dimer resembling the canonical TyrRS dimer. The C-terminal copy of the catalytic domain has lost the catalytically important HIGH and KMSKS motifs characteristic of class I aminoacyl-tRNA synthetases. Thus, the TyrRS pseudo-dimer is inherently asymmetric and contains only one functional active site, contributed by the N-terminal half, and only one functional anticodon recognition site, contributed by the C-terminal half | Leishmania major |
Synonyms | Comment | Organism |
---|---|---|
Tyrosyl-tRNA synthetase | - |
Leishmania major |
TyrRS | - |
Leishmania major |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic relationship of TyrRS sequences, schematic overview | Leishmania major |