Structural Biology of Biosynthetic Enzymes

This group is located at the Helmholtz Institute for Pharmaceutical Research Saarland (HIPS)

Natural agents have always been the best source of antibiotics. This is exemplified by success stories such as penicillin, streptomycin, erythromycin and rifamycin. But the potential of natural agents is not being tapped to the fullest extent yet. Often, this is related to the chemical synthesis being difficult and the yields of the purification of the agents from natural sources being low. Consequently, a large number of promising natural substances have been discovered, but were not developed further for clinical application, either because their chemical structure could not be changed sufficiently or because it was impossible to produce sufficient amounts of them.


Jun. Prof. Dr Jesko Köhnke

Structural biology is so fascinating, because one can see how complex processes work at the atomic level. We can use this knowledge for enzyme and natural product engineering.

Jesko Köhnke

Jesko Köhnke initially majored in biochemistry in Hannover and graduated with a Master's degree in this field in 2005. He then went on to do his doctoral work with Prof Lawrence Shapiro at Columbia University in New York. In 2010, he completed his doctoral work titled "Structural studies of neurexins and neuroligins“ and then worked as a research fellow in the laboratory of Prof James Naismith at the University of St Andrews in Scotland.

Jesko Köhnke has been the director of the junior research group, "Structural Biology of Biosynthetic Enzymes", at the Helmholtz Institute for Pharmaceutical Research (HIPS) in the German federal state of Saarland since January 2015.  


  • HIPS Infofilm (English)

    Resistance to antibiotics has become one of the major global challenges regarding infectious diseases. This is specifically the issue that is being tackled by the new Helmholtz-Institute for Pharmaceutical Research Saarland (HIPS).

  • Surface of the enzyme PurAH

    The surface of the enzyme PurAH with the two catalytic zinc ions (grey spheres) bound at the active site.

  • 3D model of the enzyme BotH

    In bottromycin, a potential antibiotic, bacteria build up a mirrored amino acid. In a study published in the journal Nature Chemical Biology, Jesko Köhnke, head of the junior research group "Structural Biology of Biosynthetic Enzymes" at the Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), describes the enzyme BotH which is necessary for this.

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