期刊
STRUCTURE
卷 10, 期 2, 页码 237-248出版社
CELL PRESS
DOI: 10.1016/S0969-2126(02)00707-4
关键词
camptothecin; DNA repair; PLD superfamily; topoisomerase I; tyrosyl-DNA phosphodiesterase
资金
- NCI NIH HHS [CA 65656] Funding Source: Medline
- NIGMS NIH HHS [GM49156] Funding Source: Medline
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 Angstrom 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.
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