Structure of bacterial ABC transporters for maltose/maltodextrins and sulfate


The family of ABC transport systems comprises a diverse class of transport proteins that couple the translocation of solutes across biological membranes to the free energy of ATP hydrolysis. Members of the family have been identified in organisms belonging to each of the three major kingdoms, some of them with medical relevance. The molecular mechanism by which these proteins exert their functions is still poorly understood, despite the recent progress in obtaining tertiary structural informations on several ATPase domains as well as, most recently, on two complete ABC transporters. Additional crystal structures will however be required to further elucidate conformational changes upon ATP binding on the molecular level and to get a more complete picture on the numerous subfamilies of ABC transporters. We propose to continue our efforts to grow crystals of the maltose transporter (MalFGK2) of Salmonella typhimurium, thereby focusing on mutant complexes. Furthermore, we will complete the biochemical characterization of the homologous transporter of Alicyclobacillus acidocaldarius and include it into the screening program. Finally, by extending our initial project, we will solve the crystal structures of the ATPase protein CysA of A. acidocaldarius in the presence and absence of ATP, and of a putative sulfate transporter, CysTA, of the archaeon Archaeoglobus fulgidus.
The family of ABC transport systems comprises a diverse class of transport proteins that couple the translocation of solutes across biological membranes to the free energy of ATP hydrolysis. Members of the family have been identified in organisms belonging to each of the three major kingdoms, some of them with medical relevance. The molecular mechanism by which these proteins exert their functions is still poorly understood, despite the recent progress in obtaining tertiary structural informations on several ATPase domains as well as, most recently, on two complete ABC transporters. Additional crystal structures will however be required to further elucidate conformational changes upon ATP binding on the molecular level and to get a more complete picture on the numerous subfamilies of ABC transporters. We will grow crystals of the maltose transporter (MalFGK2) of Salmonella typhimurium, thereby focusing on mutant complexes. Furthermore, we will solve the crystal structures of the ATPase protein CysA of A. acidocaldarius in the presence and absence of ATP, and of a putative sulfate transporter, CysTA, of the archaeon Archaeoglobus fulgidus.
The family of ABC transport systems comprises a diverse class of transport proteins that couple the translocation of solutes across biological membranes to the free energy of ATP hydrolysis. Members of the family have been identified in organisms belonging to each of the three major kingdoms, some of them with medical relevance. The molecular mechanism by which these proteins exert their functions is still poorly understood, despite the recent progress in obtaining tertiary structural informations on several ATPase domains as well as, most recently, on two complete ABC transporters. Additional crystal structures will however be required to further elucidate conformational changes upon ATP binding on the molecular level and to get a more complete picture on the numerous subfamilies of ABC transporters. We propose to continue our efforts to grow crystals of the maltose transporter (MalFGK2) of Salmonella typhimurium, thereby focusing on mutant complexes. Furthermore, we will complete the biochemical characterization of the homologous transporter of Alicyclobacillus acidocaldarius and include it into the screening program. Finally, by extending our initial project, we will solve the crystal structures of the ATPase protein CysA of A. acidocaldarius in the presence and absence of ATP, and of a putative sulfate transporter, CysTA, of the archaeon Archaeoglobus fulgidus.

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

Financer
DFG: Sachbeihilfe

Duration of project
Start date: 03/2003
End date: 02/2005

Publications
Scheffel, F., Fleischer, R., Schneider, E. (2004) Functional reconstitution of a maltose ATP-binding cassette transporter from the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius. Biochim. Biophys. Acta 1656, 57-65; Fleischer, R., Wengner, A., Scheffel, F., Landmesser, H., Schneider, E. (2005) Identification of a gene cluster encoding an arginine ATP-binding-cassette transporter in the genome of the thermophilic gram-positive bacterium Geobacillus stearothermophilus strain DSMZ 13240. Microbiology 151, 835-840; Scheffel, F., Demmer, U., Warkentin, E., Hülsmann, A., Schneider, E., ermler, U. (2005) Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius. FEBS-Lett. 579, 2953-2958

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