Crystal structure of NAD+-dependent DNA ligase: Modular architecture and functional implications

Jae Young Lee, Changsoo Chang, Hyun Kyu Song, Jinho Moon, Jin Kuk Yang, Hyun Kyu Kim, Suk Tae Kwon, Se Won Suh

Research output: Contribution to journalArticle

147 Citations (Scopus)

Abstract

DNA ligases catalyze the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD+ as a cofactor. Despite the difference in cofactor specificity and limited overall sequence similarity, the two classes of DNA ligase share basically the same catalytic mechanism. In this study, the crystal structure of an NAD+-dependent DNA ligase from Thermus filiformis, a 667 residue multidomain protein, has been determined by the multiwavelength anomalous diffraction (MAD) method. It reveals highly modular architecture and a unique circular arrangement of its four distinct domains. It also provides clues for protein flexibility and DNA-binding sites. A model for the multidomain ligase action involving large conformational changes is proposed.

Original languageEnglish
Pages (from-to)1119-1129
Number of pages11
JournalEMBO Journal
Volume19
Issue number5
Publication statusPublished - 2000 Mar 1
Externally publishedYes

Keywords

  • DNA ligase
  • Helix-hairpin-helix motif
  • Nucleotidyl transferase
  • Oligomer-binding fold
  • Zinc finger motif

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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  • Cite this

    Lee, J. Y., Chang, C., Song, H. K., Moon, J., Yang, J. K., Kim, H. K., Kwon, S. T., & Suh, S. W. (2000). Crystal structure of NAD+-dependent DNA ligase: Modular architecture and functional implications. EMBO Journal, 19(5), 1119-1129.