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

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 basical...

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Bibliographic Details
Published in:The EMBO journal 2000-03, Vol.19 (5), p.1119-1129
Main Authors: Lee, Jae Young, Chang, Changsoo, Song, Hyun Kyu, Moon, Jinho, Yang, Jin Kuk, Kim, Hyun-Kyu, Kwon, Suk-Tae, Suh, Se Won
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Deoxyribonucleic acid
DNA
DNA - metabolism
DNA ligase
DNA Ligases
helix-hairpin-helix motif
Ligases - chemistry
Ligases - metabolism
Molecular Sequence Data
nucleotidyl transferase
oligomer-binding fold
Protein Binding
Protein Conformation
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Structure-Activity Relationship
zinc finger motif
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Summary: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.
ISSN:0261-4189
1460-2075
DOI:10.1093/emboj/19.5.1119