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Experimental results should confirm or reject these models and provide new data for future bioinformatics studies to refine the models.īacterial cell division is performed at the middle of the cell, after duplication and segregation of the genetic material into the daughter nucleoids. The bioinformatics modelling of this kind of protein complex, whose function is mainly structural, provide useful information. Both models could be further stabilized by the binding of the other proteins of the divisome. Although the hexameric model 2:2:2 has features that indicate that this is the most plausible structure, the ternary complex 1:1:1 cannot be discarded. The two models obtained for the FtsB/FtsL/FtsQ complex were stable and thus compatible with the in vivo periplasmic complex structure. The nature of the protein-protein contacts was energetically favourable in both models and the overall structures were in agreement with the experimental evidence reported. Two final structurally-stable models, one trimeric and one hexameric, were obtained. The crystallographic structure of FtsQ was added to this complex, through protein-protein docking. The FtsB/FtsL subcomplex was modelled as a coiled-coil based on sequence information and several stoichiometric possibilities. coli complex were obtained from bioinformatics analysis. Two oligomeric models for the periplasmic region of the FtsB/FtsL/FtsQ E. The purpose of this study was to obtain a structural model of the periplasmic part of the FtsB/FtsL/FtsQ complex, using bioinformatics tools and experimental data reported in the literature. These components are small bitopic membrane proteins, and their specific function seems to be mainly structural. The proteins involved in connecting both steps in cell division are FtsQ, FtsB and FtsL, and their interaction is a crucial and conserved event in the division of different bacteria. In the second step, the formation of the peptidoglycan synthesis machinery in the periplasm takes place, followed by cell division. This process can be divided into two steps, in which the first is the polymerization of FtsZ to form the Z ring in the cytoplasm, and then the sequential addition of FtsA/ZipA to anchor the ring at the cytoplasmic membrane, a stage completed by FtsEX and FtsK. Bacterial division is produced by the formation of a macromolecular complex in the middle of the cell, called the divisome, formed by more than 10 proteins.