CATH Domain 4ufzA03

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.30	2-Layer Sandwich
	3.30.470	D-amino Acid Aminotransferase; Chain A, domain 1
	3.30.470.30	DNA ligase/mRNA capping enzyme

Domain Context

CATH Clusters

Superfamily	DNA ligase/mRNA capping enzyme
Functional Family

Enzyme Information

6.5.1.2

DNA ligase (NAD(+)).

based on mapping to UniProt P43813

NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.

-!- The enzyme, typically found in bacteria, 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 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. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.1, EC 6.5.1.6 and EC 6.5.1.7.

UniProtKB Entries (1)

P43813

DNLJ_HAEIN

Haemophilus influenzae Rd KW20

DNA ligase

PDB Structure

PDB	4UFZ
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Negishi Cross-Coupling Enabled Synthesis of Novel Nad(+)-Dependent DNA Ligase Inhibitors and Sar Development. Murphy-Benenato, K.E., Gingipalli, L., Boriack-Sjodin, P.A., Martinez-Botella, G., Carcanague, D., Eyermann, C.J., Gowravaram, M., Harang, J., Hale, M.R., Ioannidis, G., Jahic, H., Johnstone, M., Kutschke, A., Laganas, V.A., Loch, J.T., Miller, M.D., Oguto, H., Patel, S.J. Bioorg.Med.Chem.Lett.