Crystallization and preliminary X-ray analysis of the ATP-binding domain of the ABC transporter haemolysin B from Escherichia coli.
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.
Kránitz
László
L
Institute of Biochemistry, Biocenter N210, Johann Wolfgang Goethe University Frankfurt, Marie Curie Strasse 9, 65439 Frankfurt, Germany.
Benabdelhak
Houssain
H
Horn
Carsten
C
Blight
Mark A
MA
Holland
I Barry
IB
Schmitt
Lutz
L
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry*; D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D006460:Hemolysin Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C086257:hemolysin B