Manjula, M. and Pampa, K. J. and Madan Kumar, S. and Kunishima, Naoki and Lokanath, N. K. (2012) Purification, crystallization and preliminary X-ray diffraction studies of the ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus. Acta Crystallographica Section F, 68 (11). pp. 1406-1408. ISSN 1744-3091
Full text not available from this repository. (Request a copy)Abstract
ATP-binding cassette (ABC) transporters, also known as traffic ATPases, form a large family of integral membrane proteins responsible for the translocation of a variety of chemically diverse substrates across the lipid bilayers of cellular membranes of both prokaryotes and eukaryotes by the hydrolysis of ATP. The ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus, a homodimeric enzyme, was overexpressed in Escherichia coli and purified. Crystals were obtained using the microbatch-under-oil method at 291 K. X-ray diffraction data to 1.6 Å resolution were collected on SPring-8 beamline BL26B1. The crystals belonged to the orthorhombic space group I222, with unit-cell parameters a = 54.94, b = 78.63, c = 112.96 Å. Assuming the presence of a dimer in the asymmetric unit gave a crystal volume per protein weight (VM) of 2.32 Å3 Da−1 and a solvent content of 47%; this was consistent with the results of a dynamic light-scattering experiment, which showed a dimeric state of the protein in solution. Molecular-replacement trials using the crystal structure of HisP from the Salmonella typhimurium ATP-binding subunit of an ABC transporter as a search model did not provide a satisfactory solution, indicating that the two ATP-binding subunits of ABC transporters have substantially different structures.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ATP-binding subunit, ABC transporters, Geobacillus kaustophilus |
| Subjects: | D Physical Science > Physics |
| Divisions: | Department of > Physics |
| Depositing User: | C Swapna Library Assistant |
| Date Deposited: | 16 Aug 2019 10:05 |
| Last Modified: | 01 Dec 2022 10:13 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/6443 |
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