CATH Classification

Domain Context

CATH Clusters

Superfamily DNA ligase, ATP-dependent, N-terminal domain
Functional Family DNA ligase

Enzyme Information

6.5.1.1
DNA ligase (ATP).
based on mapping to UniProt Q980T8
ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.
-!- The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- 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)-(DNA). -!- 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. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7.

UniProtKB Entries (1)

Q980T8
DNLI_SACS2
Saccharolobus solfataricus P2
DNA ligase

PDB Structure

PDB 2HIX
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
A Flexible Interface between DNA Ligase and PCNA Supports Conformational Switching and Efficient Ligation of DNA.
Pascal, J.M., Tsodikov, O.V., Hura, G.L., Song, W., Cotner, E.A., Classen, S., Tomkinson, A.E., Tainer, J.A., Ellenberger, T.
Mol.Cell