1JY1

CRYSTAL STRUCTURE OF HUMAN TYROSYL-DNA PHOSPHODIESTERASE (TDP1)

1JY1 の概要

• エントリーDOI: 10.2210/pdb1jy1/pdb
• 分子名称: TYROSYL-DNA PHOSPHODIESTERASE (2 entities in total)
• 機能のキーワード: pld superfamily, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q9NUW8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52897.58

構造登録者

Davies, D.R.,Interthal, H.,Champoux, J.J.,Hol, W.G.J. (登録日: 2001-09-10, 公開日: 2002-02-20, 最終更新日: 2024-10-16)

主引用文献

Davies, D.R.,Interthal, H.,Champoux, J.J.,Hol, W.G.
The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1.
Structure, 10:237-248, 2002

PubMed Abstract: Tyrosyl-DNA phosphodiesterase (Tdp1) catalyzes the hydrolysis of a phosphodiester bond between a tyrosine residue and a DNA 3' phosphate. The enzyme appears to be responsible for repairing the unique protein-DNA linkage that occurs when eukaryotic topoisomerase I becomes stalled on the DNA in the cell. The 1.69 A crystal structure reveals that human Tdp1 is a monomer composed of two similar domains that are related by a pseudo-2-fold axis of symmetry. Each domain contributes conserved histidine, lysine, and asparagine residues to form a single active site. The structure of Tdp1 confirms that the protein has many similarities to the members of the phospholipase D (PLD) superfamily and indicates a similar catalytic mechanism. The structure also suggests how the unusual protein-DNA substrate binds and provides insights about the nature of the substrate in vivo.

PubMed: 11839309
DOI: 10.1016/S0969-2126(02)00707-4

実験手法

X-RAY DIFFRACTION (1.69 Å)