Bacterial ATP-driven transport systems for maltose/maltodextrins (ABC transporter)

members of the protein family of ABC (ATP-binding cassette) transporters, which have been found in all living organisms, some with medical relevance, mediate the uptake or export of solutes across biological membranes at the expense of ATP. Using the binding protein-dependent uptake systems for maltose/maltodextrins of Samonella typhimurium and Alicyclobacillus acidocaldarius as models, we study basic principles of their functions and some aspects of carbon regulation. We study

Principal investigators
Schneider, Erwin Prof. Dr. rer. nat. (Details) (Physiology of Microorganisms)

DFG: Sachbeihilfe

Duration of project
Start date: 11/2002
End date: 11/2003

Stein, A., Seifert, M., Volkmer-Engert, R., Siepelmeyer, J., jahreis, K., Schneider, E. (2002) Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit. Eur. J. Biochem. 269, 4074-4085; Landmesser, H., Stein, A., Blüschke, B., Brinkmann, M., Hunke, S., Schneider, E. (20029 Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK2) of Salmonella typhimurium. Biochim. Biophys. Acta 1565, 64-72; Schneider, E. (2003) Import of solutes by ABC transporters-the maltose and other systems, In: ABC transporters: From Bacteria to Man, pp. 157- 185, Elsevier Science Ltd; Schäfer, K., Magnusson, U., Scheffel, F., Schiefner, A., Sandgren, M.O., Diederichs, K., Welte, W., Hülsmann, A., Schneider, E., Mowbray, S. (2004) X-ray structures of the maltose-maltodextrin-binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins. J. Mol. Biol. 335, 261-274

Last updated on 2022-08-09 at 01:08