coli), this complex is recruited to the division site at the mid-cell (Fig. Exploitation of the cell division process is hence an intriguing direction but nonetheless limited by the lack of structural information of the multi-protein division machinery, called the divisome 1, 2. In the current era, with the increasing prevalence of antibiotic resistance in bacteria, antibiotics with novel mechanisms are urgently called for. These results lead us to propose a structure-based model that delineates the mechanism of the regulation of peptidoglycan synthases by the FtsBLQ complex.īacterial cell division is a fundamental process which harbors a rich source of potential antibiotic targets 1, 2.
This trimeric structure may also facilitate interactions with other divisome proteins in an allosteric manner. Such a conformation could be strengthened by the transmembrane and the coiled-coil domains of the FtsBL heterodimer, as well as an extended β-sheet of the C-terminal interaction site involving all three proteins. Here, we report the full-length structure of the heterotrimeric FtsBLQ complex, which reveals a V-shaped architecture in a tilted orientation. Yet the underlying mechanism of FtsBLQ-mediated regulation is largely unknown. This complex regulates the transglycosylation and transpeptidation activities of the FtsW-FtsI complex and PBP1b via coordination with FtsN, the trigger for the onset of constriction. The essential membrane protein complex of FtsB, FtsL and FtsQ (FtsBLQ) is at the heart of the divisome assembly cascade in Escherichia coli. The synthesis of the cell-wall peptidoglycan during bacterial cell division is mediated by a multiprotein machine, called the divisome.
0 kommentar(er)
