CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.50 | OB fold (Dihydrolipoamide Acetyltransferase, E2P) |
|
2.40.50.140 | Nucleic acid-binding proteins |
Domain Context
CATH Clusters
| Superfamily | Nucleic acid-binding proteins |
| Functional Family | DNA ligase |
Enzyme Information
| 6.5.1.6 |
DNA ligase (ATP or NAD(+)).
based on mapping to UniProt C0LJI8
(1) ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate. (2) NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.
-!- The enzymes from the archaea Thermococcus fumicolans and Thermococcus onnurineus show high activity with either ATP or NAD(+), and significantly lower activity with TTP, GTP, and CTP. -!- 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 or NAD(+), 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. -!- Different from EC 6.5.1.1, EC 6.5.1.2, and EC 6.5.1.7.
|
UniProtKB Entries (1)
| C0LJI8 |
C0LJI8_9EURY
Thermococcus sp. 1519
DNA ligase
|
PDB Structure
| PDB | 3RR5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.
Acta Crystallogr.,Sect.F
|