1Z47

Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius

Summary for 1Z47

• Entry DOI: 10.2210/pdb1z47/pdb
• Descriptor: putative ABC-transporter ATP-binding protein, CHLORIDE ION (3 entities in total)
• Functional Keywords: alpha/beta motif; beta sandwich, ligand binding protein
• Biological source: Alicyclobacillus acidocaldarius
• Total number of polymer chains: 2
• Total formula weight: 80223.92

Authors

Scheffel, F.,Demmer, U.,Warkentin, E.,Huelsmann, A.,Schneider, E.,Ermler, U. (deposition date: 2005-03-15, release date: 2005-06-07, Last modification date: 2024-02-14)

Primary citation

Scheffel, F.,Demmer, U.,Warkentin, E.,Schneider, E.,Ermler, U.
Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius
Febs Lett., 579:2953-2958, 2005

PubMed 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 2.0 Angstroms 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.

PubMed: 15893314
DOI: 10.1016/j.febslet.2005.04.017

Experimental method

X-RAY DIFFRACTION (1.9 Å)