1V9P

Crystal Structure Of Nad+-Dependent DNA Ligase

「1DGT」から置き換えられました

1V9P の概要

• エントリーDOI: 10.2210/pdb1v9p/pdb
• 関連するPDBエントリー: 1DGT
• 分子名称: DNA ligase, ZINC ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: nad+-dependent dna ligase, ligase
• 由来する生物種: Thermus filiformis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 135467.48

構造登録者

Lee, J.Y.,Chang, C.,Song, H.K.,Moon, J.,Yang, J.K.,Kim, H.K.,Kwon, S.K.,Suh, S.W. (登録日: 2004-01-27, 公開日: 2004-03-30, 最終更新日: 2023-12-27)

主引用文献

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

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: 10698952
DOI: 10.1093/emboj/19.5.1119

実験手法

X-RAY DIFFRACTION (2.9 Å)