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Structural and mechanistic conservation in DNA ligases

Nucleic Acids Res. 2000 Nov 1;28(21):4051-8. doi: 10.1093/nar/28.21.4051.

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.

Publication types

  • Editorial
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Catalysis
  • Conserved Sequence*
  • DNA Ligases / chemistry*
  • DNA Ligases / classification
  • DNA Ligases / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • NAD / metabolism
  • Protein Structure, Tertiary
  • Substrate Specificity
  • Zinc Fingers

Substances

  • NAD
  • Adenosine Triphosphate
  • DNA Ligases