CRYSTAL-STRUCTURE OF AN ATP-DEPENDENT DNA-LIGASE FROM BACTERIOPHAGE-T7

Citation
Hs. Subramanya et al., CRYSTAL-STRUCTURE OF AN ATP-DEPENDENT DNA-LIGASE FROM BACTERIOPHAGE-T7, Cell, 85(4), 1996, pp. 607-615
Citations number
44
Categorie Soggetti
Biology,"Cell Biology
Journal title
CellACNP
ISSN journal
00928674
Volume
85
Issue
4
Year of publication
1996
Pages
607 - 615
Database
ISI
SICI code
0092-8674(1996)85:4<607:COAADF>2.0.ZU;2-8
Abstract
The crystal structure of the ATP-dependent DNA ligase from bacteriopha ge T7 has been solved at 2.6 Angstrom resolution. The protein comprise s two domains with a deep cleft running between them. The structure of a complex with ATP reveals that the nucleotide binding pocket is situ ated on the larger N-terminal domain, at the base of the cleft between the two domains of the enzyme. Comparison of the overall domain struc ture with that of DNA methyltransferases, coupled with other evidence, suggests that DNA also binds in this cleft. Since this structure is t he first of the nucleotidyl-transferase superfamily, which includes th e eukaryotic mRNA capping enzymes, the relationship between the struct ure of DNA ligase and that of other nucleotidyl-transferases is also d iscussed.