Summary for 1V9P
| Entry DOI | 10.2210/pdb1v9p/pdb |
| Related | 1DGT |
| Descriptor | DNA ligase, ZINC ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | nad+-dependent dna ligase, ligase |
| Biological source | Thermus filiformis |
| Total number of polymer chains | 2 |
| Total formula weight | 135467.48 |
| Authors | Lee, J.Y.,Chang, C.,Song, H.K.,Moon, J.,Yang, J.K.,Kim, H.K.,Kwon, S.K.,Suh, S.W. (deposition date: 2004-01-27, release date: 2004-03-30, Last modification date: 2023-12-27) |
| Primary citation | Lee, J.Y.,Chang, C.,Song, H.K.,Moon, J.,Yang, J.K.,Kim, H.K.,Kwon, S.T.,Suh, S.W. Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications. Embo J., 19:1119-1129, 2000 Cited by PubMed 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. PubMed: 10698952DOI: 10.1093/emboj/19.5.1119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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