CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.50 | OB fold (Dihydrolipoamide Acetyltransferase, E2P) |
|
2.40.50.140 | Nucleic acid-binding proteins |
Domain Context
CATH Clusters
| Superfamily | Nucleic acid-binding proteins |
| Functional Family |
Enzyme Information
| 6.1.1.23 |
Aspartate--tRNA(Asn) ligase.
based on mapping to UniProt P56459
ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx).
-!- When this enzyme acts on tRNA(Asp), it catalyzes the same reaction as EC 6.1.1.12. -!- It has, however, diminished discrimination, so that it can also form aspartyl-tRNA(Asn). -!- This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. -!- This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon) and tRNA(Asn) (GUU anticodon). -!- The aspartate-tRNA(Asn) is not used in protein synthesis until it is converted by EC 6.3.5.6 into asparaginyl-tRNA(Asn).
|
UniProtKB Entries (1)
| P56459 |
SYDND_HELPY
Helicobacter pylori 26695
Aspartate--tRNA(Asp/Asn) ligase
|
PDB Structure
| PDB | 5GRO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of the N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori
Acta Crystallogr F Struct Biol Commun
|
