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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.

Böhm et al, Molecular Cell 81, 2403–2416 (2021)

Activation of translation in eukaryotes requires multisite phosphorylation of the protein 4E-BP. We employed NMR spectroscopy to study the interaction of intrinsically disordered 4E-BP1 with the TOR complex. Specific motifs within 4E-BP1 bind the TOR-subunit Raptor, resulting in avidity-based substrate tethering. Our findings also explain the differential rapamycin sensitivity of the 4E-BP1 phosphorylation.

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.

 

 

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