Conservation of FtsZ protein

FtsZ protein plays an essential role in cell division by forming a contractile ring structure at the division site, thereby controlling both the location and timing of cell division. The minimal divisome of a synthetic cell therefore also relies on FtsZ.

In this project, we will investigate the interactions of FtsZ with its (putative) protein interaction partners and lipids in silico. To that end, we will make use of bioinformatics tools such as AlphaFold and molecular dynamics (MD) simulations.

For this project, we are looking for a student interested in bioinformatics.

The project will be co-supervised by Federico Ramirez Gomez.

Cover figure: FtsZ from Escherichia coli. (PDB ID: 6UMK)

Previously in this project (BEP by Jesse Poort): We have investigated the conservation of FtsZ protein across bacterial species. We explored the similarities on sequence level, by finding homologous proteins and building a phylogenetic tree. Moreover, because proteins with even a moderate sequence similarity may have a conserved 3D structure, we explored similarity of FtsZ proteins from different organisms on 3D structure level, by comparing the overall folds as well as zooming in on specific parts of protein.