Front Cover: Activation, Structure, Biosynthesis and Bioactivity of Glidobactin‐like Proteasome Inhibitors from Photorhabdus laumondii (ChemBioChem 9/2021)

Glidobactin‐like proteasome inhibitors are regarded as promising candidates for anticancer drug development. We report the largest subset of glidobactin‐like proteasome inhibitors, which were produced and identified after the silent biosynthetic gene cluster plu1881–1877 had been activated in the native host Photorhabdus laumondii. Crystal‐structure analysis of the new glidobactin derivatives in complex with yeast proteasome core particle (yCP) suggests that the inhibition occurs primarily by covalent and irreversible binding of the inhibitors to the β5 subunit of the yCP. More information can be found in the full paper by H. B. Bode et al.