1nop
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(New page: 200px<br /><applet load="1nop" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nop, resolution 2.30Å" /> '''Crystal structure of...)
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Revision as of 20:19, 20 November 2007
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Crystal structure of human tyrosyl-DNA phosphodiesterase (Tdp1) in complex with vanadate, DNA and a human topoisomerase I-derived peptide
Overview
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.
About this Structure
1NOP is a Single protein structure of sequence from Homo sapiens with VO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a transition state mimic for Tdp1 assembled from vanadate, DNA, and a topoisomerase I-derived peptide., Davies DR, Interthal H, Champoux JJ, Hol WG, Chem Biol. 2003 Feb;10(2):139-47. PMID:12618186
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