CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.1490.70
Functional Family

Enzyme Information
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)

Trypanosoma brucei brucei TREU927
RNA-editing ligase 1, mitochondrial

PDB Structure

External Links
Organism Escherichia
Primary Citation
High resolution crystal structure of a key editosome enzyme from Trypanosoma brucei: RNA editing ligase 1.
Deng, J., Schnaufer, A., Salavati, R., Stuart, K.D., Hol, W.G.