On December 9th, Prof. Dr. Stephan Sieber (TUM Department of Chemistry) will give a talk entitled “Weak Spot in Pathogenic Bacteria – ClpX-ClpP Protein Complex Could be Starting Point for New Antibiotics”. Antibiotics are still the most important weapon for combatting bacterial infections but medical science is running out of “ammunition” because of more and more frequently occurring resistances. Professor Sieber and his team have now elucidated the three-dimensional structure of the proteolytic complex ClpX-ClpP for the first time and thereby established an important basis for future pharmacological applications. The proteolytic enzyme ClpP is a particularly promising point of attack for antibacterial therapies as it not only plays an important role in bacterial metabolism but also ensures the controlled degradation of defective proteins. For this purpose, it requires the ClpX protein as a starting aid. In the complex with ClpP, ClpX identifies proteins, which should be degraded, unfurls them and guides them into its barrel-like degradation chamber.
In addition to the degradation of defective proteins, ClpP is also a decisive regulator in the production of an arsenal of bacterial toxins, which are primarily responsible for the pathogenic effect of many pathogens. After researching the ClpP protease for years, Sieber and his team have already developed a large number of potent inhibitors against ClpP and ClpX which stop the production of bacterial toxins and can therefore more or less disarm them (TUM press release).
Publication
Gatsogiannis, C., Balogh, D., Merino F., Sieber S. A., Raunser, S., “Cryo-EM structure of the ClpXP protein degradation machinery”. Nature Structural & Molecular Biology (2019); DOI: 10.1038/s41594-019-0304-0.
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