CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.1490.70
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.

UniProtKB Entries (1)

P32277
RLIG2_BPT4
Escherichia virus T4
RNA ligase 2

PDB Structure

PDB 2HVR
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
RNA Ligase Structures Reveal the Basis for RNA Specificity and Conformational Changes that Drive Ligation Forward.
Nandakumar, J., Shuman, S., Lima, C.D.
Cell(Cambridge,Mass.)