CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.3550 | eoxyguanosinetriphosphate triphosphohydrolase fold |
|
1.10.3550.20 |
Domain Context
CATH Clusters
| Superfamily | 1.10.3550.20 |
| Functional Family | T4 RNA ligase 1 |
Enzyme Information
| 6.5.1.3 |
RNA ligase (ATP).
based on mapping to UniProt P00971
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)
| P00971 |
RLIG_BPT4
Escherichia virus T4
T4 RNA ligase 1
|
PDB Structure
| PDB | 5TT6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Two-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NAD(+)-dependent polynucleotide ligases.
Proc. Natl. Acad. Sci. U.S.A.
|
