Health
Research provides insights into bacterial natural product molecular factories
The active agents of many drugs are so-called natural products, because only microorganisms are often able to produce complex structures. Similar to factory production lines, large enzyme complexes bring these activator molecules together. The teams at the Technical University of Munich (TUM) and the Goethe University of Frankfurt have succeeded in investigating the basic mechanism of one of these molecular factories.
Many important drugs, such as antibiotics and active agents against cancer, are natural products made by microorganisms such as bacteria and fungi. In the lab, these natural products are often not produced at all or only with great effort. Many starting points for such compounds are polyketides. Polyketides are carbon chains that are double-bonded to the oxygen atom every second atom.
It is produced in microbial cells such as Photorhabdus luminescens bacteria with the help of polyketide synthase (PKS). To build the molecule of interest step by step, the first step in the PKS type II system is to bring four proteins together into a “team”.
In the second step, they are further enzymatically modified to the desired natural product. Examples of bacterial natural products produced in that way are, inter alia, clinically used tetracycline antibiotics or doxorubicin, anticancer agents.
Interdisciplinary cooperation
The modified step of the second stage has been well studied for many active agents, but to date, the first stage of these molecular factories in which highly reactive polyketide intermediates are attached to the enzyme complex has been investigated. There was little insight into its general functioning, and it is protected against natural reactions.
This gap is closed as a result of a collaboration between the working group of Michael Groll, a professor of biochemistry at the Technical University of Munich, and Helg Bode, a professor of molecular biotechnology at the University of Goethe in Frankfurt. Natural chemistry..
Discovery Inspires New Synthesis of Activators
In connection with this work, for the first time, we have analyzed the complex of various partner proteins of the type II polyketide synthase with the aid of X-ray structural analysis, in order to gain a detailed understanding of the complete catalytic cycle. became. “
Michael Groll, Professor of Biochemistry, Technical University of Munich
“Based on these findings, it will be possible in the future to target and manipulate central biochemical processes, thus altering the basic structure instead of being restricted to decorative enzymes,” Helge Bode. He adds.
While developing improved antibiotics and other drugs has come a long way, both groups have been optimistic and have also been able to explain the structure and mechanism of the missing parts of molecular factories. “We already have promising data for additional protein complexes,” says Maximilian Schmalhofer, a PhD candidate involved in research at Munich.
This work was funded by the German Forschungs Mainshaft (DFG), with the excellence of the SPP 1617, SFB 1035, and the Integrated Protein Science Munich (CIPSM) cluster, and LOEWE’s focus on MegaSyn, Hesse. Supported X-ray structural data were measured at the Paul Scherrer Institute in Villigen (Switzerland). The Swedish national computing infrastructure provided computing time for theoretical modeling.
Source:
See journal:
Broyer, A. , other (2020) Structural snapshot of the minimal PKS system involved in octaketide biosynthesis. Natural chemistry.. doi.org/10.1038/s41557-020-0491-7..
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