Institute of Structural Biology
University of Bonn

There it is, the long awaited structure of a TRAP transporter. Our cryo EM structure of the sialic acid transporter HiSiaPQM finally reveals the function of the enigmatic Q-domain and how the membrane domains of TRAPs are structurally and conformationally coupled to their soluble substrate binding protein. This is the result of an eight years journey and a fantastic collaboration with Gavin Thomas from the University of York. As a cherry on the cake, single molecule studies with the lab of Uli Kubitscheck in Bonn provide the first real-time glimps of the transporter in action. The study has just been published in Nature Communications....

Following the movement of a protein is often extremely important to understand its function. Membrane transporters, for example, undergo a series of complicated movements to translocate a substrate. Two techniques that are often used to study such movements are PELDOR/DEER and smFRET. Both techniques can measure distances on the nanometer scale. In collaboration with the laboratory of Thorben Cordes at the LMU Munich, Martin and Gregor have compared the accuracy of the two methods on three different substrate binding proteins. The study has just been published in Nature Communications....

The long-awaited structure of full-length, human NLRP3 is here! Inga and colleagues have done a great job determining the cryo-EM structure of this inflammasomal protein in the inactive state bound to the inhibitor CRID3. In solution, the protein forms a decamer composed as pentamer of dimers. We identify a binding site that ties together five subdomains to keep the protein locked in the inactive state. This structure opens a wide field for optimization and development of other inflammation-targeting inhibitors as new medicines. Read the full story here....