Crystallization and preliminary X-ray analysis of AlgS, a bacterial ATP-binding cassette (ABC) protein specific to macromolecule import.
Sphingomonas sp. A1 possesses a macromolecule (alginate; average molecular size 25 700 Da) uptake system mediated by a novel pit-dependent ABC transporter. In this system, AlgS (363 amino-acid residues; 40 kDa) functions as an ATPase and provides energy for the translocation of high molecular-weight alginate across the cytoplasmic membrane. Hexahistidine-tagged AlgS of Sphingomonas sp. A1 was overexpressed in Escherichia coli and crystallized by means of the hanging-drop vapour-diffusion method with ammonium dihydrogen monophosphate as the precipitant. Preliminary X-ray analysis of the resultant crystals was performed; they belonged to the monoclinic space group P2(1) and had unit-cell parameters a = 57.4, b = 92.7, c = 65.8 A, beta = 102.3 degrees. X-ray diffraction data to 3.2 A have been collected from the native crystal.
Mishima
Y
Y
Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011, Japan.
Momma
K
K
Hashimoto
W
W
Mikami
B
B
Murata
K
K
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry*; D000251:Adenosine Triphosphatases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D046911:Macromolecular Substances; D011487:Protein Conformation; D020578:Sphingomonas / Q000737:chemistry*
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D046911:Macromolecular Substances; D000251:Adenosine Triphosphatases; C411336:AlgS protein, Sphingomonas