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• W2091859537 abstract "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. 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. The conformation of the bound substrate mimic gives compelling evidence that the topoisomerase I-DNA complex must undergo extensive modification prior to cleavage by Tdp1. The structure also illustrates that the use of vanadate as the central moiety in high-order complexes has the potential to be a general method for capturing protein-substrate interactions for phosphoryl transfer enzymes, even when the substrates are large, complicated, and unusual." @default.
• W2091859537 created "2016-06-24" @default.
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• W2091859537 date "2003-02-01" @default.
• W2091859537 modified "2023-10-16" @default.
• W2091859537 title "Crystal Structure of a Transition State Mimic for Tdp1 Assembled from Vanadate, DNA, and a Topoisomerase I-Derived Peptide" @default.
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• W2091859537 doi "https://doi.org/10.1016/s1074-5521(03)00021-8" @default.
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