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Crystallization and preliminary X-ray crystallographic studies on the parD-encoded protein Kid from Escherichia coli plasmid R1

By D. Hargreaves, R. Giraldo, S. Santos-Sierra, R. Boelens, D.W. Rice, R. Díaz Orejas and J.B. Rafferty


DNA replication in Escherichia coli and therefore bacterial proliferation relies upon the efficient functioning of the DnaB helicase. The toxin protein Kid from the plasmid-stability system parD encoded on plasmid R1 of E. coli is thought to target and block DnaB-dependent DNA replication. The toxicity of Kid is antagonized through interaction with the Kis antidote protein and the resultant complex can then act as a transcriptional regulator for the parD system. Crystals of selenomethionine-incorporated Kid have been obtained by the hanging-drop vapour-diffusion method using potassium phosphate as the precipitant. The crystals belong to the monoclinic system, space group P21, have unit-cell parameters a = 32.9, b = 45.0, c = 64.4 Å, β = 96.2° and diffract to a dmin of better than 1.8 Å on a synchrotron-radiation source. The determination of the structure of Kid will permit a better understanding of its interactions with DnaB and Kis and allow the evolutionary relationships of Kid to other toxins of plasmid and chromosomal origin to be explored

Year: 2002
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