1JY1

CRYSTAL STRUCTURE OF HUMAN TYROSYL-DNA PHOSPHODIESTERASE (TDP1)

Summary for 1JY1

• Entry DOI: 10.2210/pdb1jy1/pdb
• Descriptor: TYROSYL-DNA PHOSPHODIESTERASE (2 entities in total)
• Functional Keywords: pld superfamily, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9NUW8
• Total number of polymer chains: 1
• Total formula weight: 52897.58

Authors

Davies, D.R.,Interthal, H.,Champoux, J.J.,Hol, W.G.J. (deposition date: 2001-09-10, release date: 2002-02-20, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.69 Å)