Structure of bacterial ABC transporters for maltose/maltodextrins and sulfate

• Antragsteller: Professor Dr. Erwin Schneider
• Fachliche Zuordnung: Stoffwechselphysiologie, Biochemie und Genetik der Mikroorganismen
• Förderung: Förderung von 1999 bis 2011
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 5172202

The family of ABC transport systems comprises a diverse class of transport proteins that couple the energy of ATP hydrolysis to the translocation of solutes across biological membranes. Members of the family have been identified in organisms belonging to each of the three major kingdoms, some of them with medical relevance (antibiotic and multidrug resistance, cystic fibrosis). The molecular mechanism by which these proteins exert their functions is still poorly understood, mainly due to the lack of tertiary structural informations. By using the well-studied ABC transport system for maltose (Ma1FGK2) of salmonella typhimurium as a mode, we will contribute to the investigations of the field. First, we will solve the structure of the ATP-binding subunit Ma1K by X-ray diffraction analysis of available crystals. Complementary to these studies we will determine the solution structure of a C-terminal Ma1K fragment by NMR. In a second set of experiments we will attempt to obtain 2D- and 3D-crystals of the purified Ma1FGK2 complex. Analysis of the preparation by electron microscopy and the production of 2D crystals will provide additional structural informations. Finally, a homologous transport system from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius will be studied as an alternative, thereby taking advantage from its increased protein stability in crystallization experiments.

• DFG-Verfahren: Schwerpunktprogramme
• Teilprojekt zu: SPP 1070: Struktur funktioneller Module von energiewandelnden Systemen in Prokaryoten
• Beteiligte Person: Privatdozent Dr. Ulrich Ermler