Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome

Hong Thuy Vy Nguyen, Xiaorui Chen, Claudia Parada, An-Chi Luo, Orion Shih, U-Ser Jeng, Chia-Ying Huang, Yu-Ling Shih () and Che Ma ()
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Hong Thuy Vy Nguyen: Genomics Research Center, Academia Sinica
Xiaorui Chen: Genomics Research Center, Academia Sinica
Claudia Parada: Institute of Biological Chemistry, Academia Sinica
An-Chi Luo: National Taiwan University
Orion Shih: National Synchrotron Radiation Research Center
U-Ser Jeng: National Synchrotron Radiation Research Center
Chia-Ying Huang: Paul Scherrer Institute
Yu-Ling Shih: National Taiwan University
Che Ma: Genomics Research Center, Academia Sinica

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract The synthesis of the cell-wall peptidoglycan during bacterial cell division is mediated by a multiprotein machine, called the divisome. The essential membrane protein complex of FtsB, FtsL and FtsQ (FtsBLQ) is at the heart of the divisome assembly cascade in Escherichia coli. 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. Yet the underlying mechanism of FtsBLQ-mediated regulation is largely unknown. Here, we report the full-length structure of the heterotrimeric FtsBLQ complex, which reveals a V-shaped architecture in a tilted orientation. 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. This trimeric structure may also facilitate interactions with other divisome proteins in an allosteric manner. These results lead us to propose a structure-based model that delineates the mechanism of the regulation of peptidoglycan synthases by the FtsBLQ complex.

Date: 2023
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DOI: 10.1038/s41467-023-37543-4

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