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- Title
Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius
- Authors
Scheffel, Frank; Demmer, Ulrike; Warkentin, Eberhard; Hülsmann, Anja; Schneider, Erwin; Ermler, Ulrich
- Abstract
Abstract: CysA, the ATPase subunit of a putative sulfate ATP-binding cassette transport system of the gram-positive thermoacidophilic bacterium Alicyclobacillus acidocaldarius, was structurally characterized at a resolution of 2.0Å in the absence of nucleotides. In line with previous findings on ABC-ATPases the structures of the two monomers (called CysA-1 and CysA-2) in the asymmetric unit differ substantially in the arrangement of their individual (sub)domains. CysA-2 was found as a physiological dimer composed of two crystallographically related monomers that are arranged in an open state. Interestingly, while the regulatory domain of CysA-2 packs against its opposing domain that of CysA-1 undergoes a conformational change and, in the dimer, would interfere with the opposing monomer thereby preventing solute translocation. Whether this conformational state is used for regulatory purposes will be discussed.
- Subjects
ADENOSINE triphosphatase; ESCHERICHIA coli; ESCHERICHIA coli O157:H7; CHEMICALS
- Publication
FEBS Letters, 2005, Vol 579, Issue 13, p2953
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2005.04.017