Download MendeleyThe crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1.
Davies, D.R., Interthal, H., Champoux, J.J., Hol, W.G.(2002) Structure 10: 237-248
- PubMed: 11839309
- DOI: https://doi.org/10.1016/s0969-2126(02)00707-4
- Primary Citation of Related Structures:
1JY1 - 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.
Organizational Affiliation:
Department of Biochemistry, Box 357742, University of Washington, Seattle, WA 98195, USA.
