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Crystal structure of NAD + ‐dependent DNA ligase: modular architecture and functional implications
Author(s) -
Lee Jae Young,
Chang Changsoo,
Song Hyun Kyu,
Moon Jinho,
Yang Jin Kuk,
Kim HyunKyu,
Kwon SukTae,
Suh Se Won
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.5.1119
Subject(s) - library science , chemistry , political science , computer science
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.