Many important natural products such as antibiotics, immunosuppressants, or cancer drugs are derived from microorganisms.

With regard to the NRPS, a specific amino acid is incorporated and processed at each station (module), so that in the end peptides emerge that can be linear, cyclic or otherwise modified including unusual amino acids.

These are small regions at the end of the assembly lines that fit with the next NRPS enzyme in line like a key in a lock.

The research groups led by Professor Jens Wöhnert form the Institute of Molecular Biosciences and Professor Helge Bode from Molecular Biotechnology at Goethe University have now been able to successfully explain this.

"We were able to determine the structures of individual docking domains and, for the first time, an NRPS docking domain pair as well," explains Carolin Hacker, who is a PhD student in Jens Wöhnert's group.

The first results on the structures of additional docking domains are quite promising.

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