title: Structural and mechanistic conservation in DNA ligases.
abstract: DNA ligases are enzymes required for the repair, replication and recombination of DNA. DNA ligases catalyse the formation of phosphodiester bonds at single-strand breaks in double-stranded DNA. Despite their occurrence in all organisms, DNA ligases show a wide diversity of amino acid sequences, molecular sizes and properties. The enzymes fall into two groups based on their cofactor specificity, those requiring NAD(+) for activity and those requiring ATP. The eukaryotic, viral and archael bacteria encoded enzymes all require ATP. NAD(+)-requiring DNA ligases have only been found in prokaryotic organisms. Recently, the crystal structures of a number of DNA ligases have been reported. It is the purpose of this review to summarise the current knowledge of the structure and catalytic mechanism of DNA ligases.
authors.affiliation: Structural Medicine Unit, Department of Haematology, Wellcome Trust Centre for Molecular Mechanisms in Disease, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK. ajd42@cam.ac.uk
authors.forename: A J
authors.initials: AJ
authors.lastname: Doherty
authors.forename: S W
authors.initials: SW
authors.lastname: Suh
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D017124:Conserved Sequence; D011088:DNA Ligases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D016335:Zinc Fingers
chemical_list: D009243:NAD; D000255:Adenosine Triphosphate; D011088:DNA Ligases