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 |
Enzyme Information
6.5.1.3 |
RNA ligase (ATP).
based on mapping to UniProt P32277
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.
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UniProtKB Entries (1)
P32277 |
RLIG2_BPT4
Escherichia virus T4
RNA ligase 2
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PDB Structure
PDB | 1S68 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Structure and mechanism of RNA ligase.
Structure
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