- Entfällt - The NRPS assembly line machinery

Prof. Dr. Mohamed A. Marahiel

Philipps University Marburg



Großer Hörsaal Erbertstraße

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A widespread class of therapeutically important natural products is of peptidic origin. Such peptides are either assembled on the ribosome and extensively post-translationally modified or are produced independent of the ribosome (non-ribosomally) using large multi-modular enzymes, the so-called non-ribosomal peptide synthetases (NRPS). Crystal and NMR structures of individual NRPS domains associated with substrate selection and activation (A-domain), substrate shuffling between active sites (PCP-domain), building block condensation (C-domain) and product release (TE-domain) have provided important insights into the catalytic mechanisms of these domains as well as their architectures and dynamics. However, structural elucidation of individual catalytic units cannot reveal how the catalytic domains are oriented and connected to each other in the context of the 3D structure of an intact NRPS. The information obtained on multi-domain NRPS module structures and their dynamics during catalysis is crucial to our understanding of how the covalently bound substrates are correctly shuffled between the catalytic centers and how domain movement is coordinated.