CATH Domain 4glxA01

CATH Classification

Level	CATH Code	Description
	1	Mainly Alpha
	1.10	Orthogonal Bundle
	1.10.287	Helix Hairpins
	1.10.287.610	Helix hairpin bin

Domain Context

CATH Clusters

Superfamily	Helix hairpin bin
Functional Family	DNA ligase

Enzyme Information

6.5.1.2

DNA ligase (NAD(+)).

based on mapping to UniProt P15042

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)

P15042

DNLJ_ECOLI

Escherichia coli K-12

DNA ligase

PDB Structure

PDB	4GLX
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Structure-guided design, synthesis and biological evaluation of novel DNA ligase inhibitors with in vitro and in vivo anti-staphylococcal activity. Surivet, J.P., Lange, R., Hubschwerlen, C., Keck, W., Specklin, J.L., Ritz, D., Bur, D., Locher, H., Seiler, P., Strasser, D.S., Prade, L., Kohl, C., Schmitt, C., Chapoux, G., Ilhan, E., Ekambaram, N., Athanasiou, A., Knezevic, A., Sabato, D., Chambovey, A., Gaertner, M., Enderlin, M., Boehme, M., Sippel, V., Wyss, P. Bioorg.Med.Chem.Lett.