Sven Sowa is a postdoctoral researcher the University of Basel since 2023 specializing in the structural and functional analysis of enzymes involved in antibiotic biosynthesis. He earned his Bachelor's degree in 2014 from the University of Leipzig, Germany, where his thesis focused on the molecular cloning of a modular pTXB1 vector encoding cytochrome P450 domains. Also at the University of Leipzig, he completed his Master's degree in 2016, working on the characterization of the final steps of the biosynthesis of cofactor F₄₃₀ in methanogenic archaea.

In 2022, Sven obtained his PhD from the University of Oulu, Finland. His doctoral research centered on the molecular mechanisms of tankyrase function and inhibition, investigating functional and structural aspects of the human ADP-ribosyltransferases TNKS1 and TNKS2. He also contributed to assay development and the structure-guided discovery of small-molecule inhibitors for various ADP-ribosyltransferases and ADP-ribosyl binding proteins.

Currently, Sven studies the mechanisms of key enzymes involved in the biosynthesis of bacterial antibiotics such as rubromycins and tropolones. He investigates the molecular basis for the potent antibiotic activity displayed by rubromycins, employing protein X-ray crystallography to gain structural insights into these enzymes. His work aims to advance the understanding of antibiotic biosynthesis, which could lead to the development of new therapeutic agents.

Publication(s):

Sowa et al. (2021): A molecular toolbox for ADP-ribosyl binding proteins. Cell Reports Methods, 1 (8), p. 100121. Available at: https://doi.org/10.1016/j.crmeth.2021.100121.

Sowa and Lehtiö (2022): The zinc-binding motif in tankyrases is required for the structural integrity of the catalytic ADP-ribosyltransferase domain. Open Biology, 12, p. 210365. Available at: https://doi.org/10.1098/rsob.210365.

Moore et al. (2017): Elucidation of the biosynthesis of the methane catalyst coenzyme F₄₃₀. Nature, 543, p. 78-82. Available at: https://doi.org/10.1038/nature21427.