Title : Crystal structure of a transition state mimic for Tdp1 assembled from vanadate, DNA, and a topoisomerase I-derived peptide.

Pub. Date : 2003 Feb

PMID : 12618186






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Tyrosyl-DNA phosphodiesterase (Tdp1) is a member of the phospholipase D superfamily and acts as a DNA repair enzyme that removes stalled topoisomerase I- DNA complexes by hydrolyzing the bond between a tyrosine side chain and a DNA 3" phosphate. Tyrosine tyrosyl-DNA phosphodiesterase 1 Homo sapiens
2 Despite the complexity of the substrate of this phosphodiesterase, vanadate succeeded in linking human Tdp1, a tyrosine-containing peptide, and a single-stranded DNA oligonucleotide into a quaternary complex that mimics the transition state for the first step of the catalytic reaction. Tyrosine tyrosyl-DNA phosphodiesterase 1 Homo sapiens