Kaur, Jakob et al, Nature 593, 125–129 (2022)

We identified the mode of action of darobactin, a natural antibiotic that inhibits the insertase BamA in Gram-negative bacteria. Darobactin binds to the lateral gate of BamA via backbone contacts. It is therefore particularly robust against resistance mutations. Our results identify the lateral gate as a functional hotspot in BamA and will facilitate the rational design of novel antibiotics.

Burmann et al, Nature 577, 127–132 (2020)

We have systematically investigated how molecular chaperones interact with the intrinsically disordered protein α-synuclein. α-synuclein plays a key role in Parkinson’s disease. We could show that molecular chaperones have a specific interaction signature and used this signature to elucidate how chaperones regulate the state of α-synuclein in living cells.

Mas et al, Science Advances 6, eabc5822 (2020)

The molecular chaperone Skp transports outer membrane proteins in Gram-negative bacteria. Using NMR spectroscopy, we showed that Skp activity is modulated through a monomer-trimer transition, where the monomeric is unfolded. Native client proteins contact all three subunits simultaneously to trimerize Skp. Skp is a unique example how chaperone activity is regulated as a function of the presence of client proteins.