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Nucleic Acids Research, 2000, Vol. 28, No. 21 4051-4058
© 2000 Oxford University Press

Survey and Summary

Structural and mechanistic conservation in DNA ligases

Aidan J. Doherty* and Se Won Suh1

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 and 1Center for Molecular Catalysis, Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 15-742, Korea

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.

* To whom correspondence should be addressed. Tel: +44 1223 762659; Fax: +44 1223 336827; Email: ajd42@cam.ac.uk


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