CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.470 | D-amino Acid Aminotransferase; Chain A, domain 1 |
|
3.30.470.30 | DNA ligase/mRNA capping enzyme |
Domain Context
CATH Clusters
| Superfamily | DNA ligase/mRNA capping enzyme |
| Functional Family | Mitochondrial RNA ligase 1 |
Enzyme Information
| 6.5.1.3 |
RNA ligase (ATP).
based on mapping to UniProt P86927
ATP + (ribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(ribonucleotide)(m) = (ribonucleotide)(n+m) + AMP + diphosphate.
-!- The enzyme catalyzes the ligation of RNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in RNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(RNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
|
UniProtKB Entries (1)
| P86927 |
RLGM1_TRYB2
Trypanosoma brucei brucei TREU927
RNA-editing ligase 1, mitochondrial
|
PDB Structure
| PDB | 1XDN |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
High resolution crystal structure of a key editosome enzyme from Trypanosoma brucei: RNA editing ligase 1.
J.Mol.Biol.
|
