CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.30 | 2-Layer Sandwich | |
3.30.1490 | Dna Ligase; domain 1 | |
3.30.1490.70 |
Domain Context
CATH Clusters
Superfamily | 3.30.1490.70 |
Functional Family | RNA-editing ligase 1, mitochondrial |
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.
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UniProtKB Entries (1)
P86927 |
RLGM1_TRYB2
Trypanosoma brucei brucei TREU927
RNA-editing ligase 1, mitochondrial
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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.
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