3GDE

The closed conformation of ATP-dependent DNA ligase from Archaeoglobus fulgidus

3GDE の概要

• エントリーDOI: 10.2210/pdb3gde/pdb
• 分子名称: DNA ligase, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: atp-dependent dna ligase, dna-binding domain, adenylation domain, ob-fold domain, atp-binding, cell cycle, cell division, dna damage, dna recombination, dna repair, dna replication, ligase, nucleotide-binding
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64310.91

構造登録者

Kim, D.J.,Kim, H.-W.,Kim, O.,Kim, H.S.,Lee, S.J.,Suh, S.W. (登録日: 2009-02-24, 公開日: 2009-12-15, 最終更新日: 2023-11-01)

主引用文献

Kim, D.J.,Kim, O.,Kim, H.-W.,Kim, H.S.,Lee, S.J.,Suh, S.W.
ATP-dependent DNA ligase from Archaeoglobus fulgidus displays a tightly closed conformation
Acta Crystallogr.,Sect.F, 65:544-550, 2009

PubMed Abstract: DNA ligases join the breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 3'-hydroxyl and 5'-phosphate termini. They fall into two classes that require either ATP or NAD(+) as the source of an AMP group that is covalently attached to a strictly conserved lysine. Conformational flexibility is essential for the function of multi-domain DNA ligases because they must undergo large conformational changes involving domain rearrangements during the course of the reaction. In the absence of the nicked DNA substrate, both open and closed conformations have been observed for the ATP-dependent DNA ligases from Sulfolobus solfataricus and Pyrococcus furiosus. Here, the crystal structure of an ATP-dependent DNA ligase from Archaeoglobus fulgidus has been determined in the DNA-unbound unadenylated state. It resembles the closed conformation of P. furiosus DNA ligase but was even more closed, thus enhancing our understanding of the conformational variability of these enzymes.

PubMed: 19478428
DOI: 10.1107/S1744309109017485

実験手法

X-RAY DIFFRACTION (2.3 Å)