AIMMS researchers discover structural interaction between the bacterial cell division proteins FtsQ and FtsB
The researchers show for the first time in atomic detail how FtsQ interacts with its downstream partner FtsB within the divisome, a protein complex that is responsible for cell division.
10/22/2018 | 10:08 AM
In most bacteria and archaea, 10 to 20 proteins are sequentially recruited at the division site to assemble in a structure that is known as the divisome. The divisome is thought to facilitate many of the steps required to make two cells out of one. FtsQ and FtsB are part of the divisome, with FtsQ being a central hub, interacting with most of the other divisome components.
The protein complex represents an exciting target for structure-based design of protein interaction inhibitors shutting down cell division. The inhibitors could be small compounds, but also peptides or peptide mimetics, as the FtsQ-FtsB interaction surface is small and the interaction is easily interrupted by single mutations.
The group of researchers, that discovered the interaction between FtsQ and FtsB, is a complex assembly in itself including members of different AIMMS groups (Molecular Microbiology, Molecular toxicology, Organic Chemistry, and Medicinal Chemistry), former neighbors from the UvA (Bacterial Cell Biology) and the MRC Laboratory of Molecular Biology in Cambridge.
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