1A0I

ATP-DEPENDENT DNA LIGASE FROM BACTERIOPHAGE T7 COMPLEX WITH ATP

1A0I の概要

• エントリーDOI: 10.2210/pdb1a0i/pdb
• 分子名称: DNA LIGASE, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: ligase, dna replication
• 由来する生物種: Enterobacteria phage T7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40395.68

構造登録者

Subramanya, H.S.,Doherty, A.J.,Ashford, S.R.,Wigley, D.B. (登録日: 1997-12-01, 公開日: 1998-03-25, 最終更新日: 2024-02-07)

主引用文献

Subramanya, H.S.,Doherty, A.J.,Ashford, S.R.,Wigley, D.B.
Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7.
Cell(Cambridge,Mass.), 85:607-615, 1996

PubMed Abstract: The crystal structure of the ATP-dependent DNA ligase from bacteriophage T7 has been solved at 2.6 A resolution. The protein comprises two domains with a deep cleft running between them. The structure of a complex with ATP reveals that the nucleotide binding pocket is situated on the larger N-terminal domain, at the base of the cleft between the two domains of the enzyme. Comparison of the overall domain structure with that of DNA methyltransferases, coupled with other evidence, suggests that DNA also binds in this cleft. Since this structure is the first of the nucleotidyltransferase superfamily, which includes the eukaryotic mRNA capping enzymes, the relationship between the structure of DNA ligase and that of other nucleotidyltransferases is also discussed.

PubMed: 8653795
DOI: 10.1016/S0092-8674(00)81260-X

実験手法

X-RAY DIFFRACTION (2.6 Å)