Bochum, 11.7.2012 No. 242
Tracked step for step ATP splitting in membrane protein dynamically measured for the first time RUB researchers report in the Journal of Biological Chemistry
How a transport protein obtains its driving force from the energy storage molecule ATP, has been tracked dynamically by RUB researchers. Using time-resolved infrared spectroscopy, they measured the structural changes in the bacterial membrane protein MsbA and its interaction partner ATP. The researchers led by Prof. Dr. Eckhard Hofmann and Prof. Dr. Klaus Gerwert from the Biophysics Department report on the results in the current issue of the Journal of Biological Chemistry.
Transport proteins are associated with various diseases
ABC transporters are membrane proteins that transport various substances from one side of the cell membrane to the other. The driving force for this is provided by the molecule ATP, a universal energy storage of the cells. ATP has three phosphate groups. If one of these splits off, energy is released. The transporters are of great medical significance as they play a central role in the multi-drug resistance of cancer cells to chemotherapeutic substances and are associated with various inherited diseases like cystic fibrosis. In recent years, researchers have uncovered the 3D structures of several of these transporters at the atomic level. Although the architecture of the nanomachines is known, a detailed understanding of how the splitting of the energy carrier ATP dynamically enables the transport of various substances across biological membranes has so far been lacking.
Protein controls ATP splitting
The Bochum researchers have now dynamically tracked the ATP splitting, called hydrolysis, for the first time in the fat transporter MsbA from the bacterium Escherichia coli. Using fourier transform infrared spectroscopy, they studied the motor domains of MsbA, i.e. the part
|Contact: Prof. Dr. Eckhard Hofmann|