CATH Classification

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.
Unciuleac, M.C., Goldgur, Y., Shuman, S.
Proc. Natl. Acad. Sci. U.S.A.