Crystallization and preliminary X-ray analysis of the ATP-binding domain of the ABC transporter haemolysin B from Escherichia coli.

Abstract

Haemolysin B (HlyB) is a transmembrane protein which belongs to the superfamily of ABC transporters. In vivo, it mediates the non-classical translocation of the 107 kDa toxin HlyA across both membranes of Escherichia coli together with haemolysin D and the outer membrane protein TolC. The cytosolic ATP-binding domain of HlyB has been overexpressed and purified as an N-terminal His-tag fusion protein. Here, the crystallization of the ATPase domain of HlyB in the presence of ATP is described. A native data set has been obtained at a resolution of 2.8 A. Crystals belong to the primitive tetragonal space group P4(x)2(1)2, where x is very likely to be 1 or 3, with unit-cell parameters a = b = 104.6, c = 125.8 A, alpha = beta = gamma = 90 degrees.

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@article{Krnitz2002CrystallizationAP, title={Crystallization and preliminary X-ray analysis of the ATP-binding domain of the ABC transporter haemolysin B from Escherichia coli.}, author={L{\'a}szl{\'o} Kr{\'a}nitz and Houssain Benabdelhak and Carsten Horn and Mark A Blight and Ian Barry Holland and Lutz Schmitt}, journal={Acta crystallographica. Section D, Biological crystallography}, year={2002}, volume={58 Pt 3}, pages={539-41} }