PMID:11856849

Citation	Kránitz, L, Benabdelhak, H, Horn, C, Blight, MA, Holland, IB and Schmitt, L (2002) Crystallization and preliminary X-ray analysis of the ATP-binding domain of the ABC transporter haemolysin B from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58:539-41
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.
Links	PubMed
Keywords	ATP-Binding Cassette Transporters/chemistry; Adenosine Triphosphatases/chemistry; Adenosine Triphosphate/metabolism; Bacterial Proteins/chemistry; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Hemolysin Proteins/chemistry; Protein Conformation; Protein Structure, Tertiary
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.