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

@article{Lee00b, 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.}, author = {Lee, J. Y. and Chang, C. and Song, H. K. and Moon, J. and Yang, J. K. and Kim, H. K. and Kwon, S. T. and Suh, S. W.}, citeulike-article-id = {388937}, journal = {EMBO J}, keywords = {crystal\_structure, enzyme, ligase, mechanism}, number = {5}, pages = {1119--29}, posted-at = {2005-11-11 16:23:16}, priority = {2}, title = {Crystal structure of NAD+-dependent DNA ligase: modular architecture and functional implications.}, volume = {19}, year = {2000} }

TY - JOUR ID - Lee00b L3 - citeulike-article-id:388937 N2 - 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. IS - 5 JF - EMBO J EP - 29 TI - Crystal structure of NAD+-dependent DNA ligase: modular architecture and functional implications. VL - 19 SP - 1119 KW - crystal_structure KW - enzyme KW - ligase KW - mechanism AU - Lee, JY AU - Chang, C AU - Song, HK AU - Moon, J AU - Yang, JK AU - Kim, HK AU - Kwon, ST AU - Suh, SW PY - 2000/// ER -