ArticleNature communications2023
Conformational changes in the essential E. coli septal cell wall synthesis complex suggest an activation mechanism.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- RodZ acts through MreBCD to activate the elongasome inJournal of bacteriology · 2026Article
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.bioRxiv : the preprint server for biology · 2026Article
- The lytic transglycosylase MltA participates in turnover of septal peptidoglycan inbioRxiv : the preprint server for biology · 2026Article
- In Silico Druggability Assessment ofAntibiotics (Basel, Switzerland) · 2026Article
- A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025Review
- Uropathogenic Escherichia coli proliferate as a coccoid morphotype inside human host cells.PLoS biology · 2025Article
- FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli.Nature microbiology · 2025Article
- Article
- Regulating cellular metabolism and morphology to achieve high-yield synthesis of hyaluronan with controllable molecular weights.Nature communications · 2025Article
- Septal wall synthesis is sufficient to change ameba-like cells into uniform oval-shaped cells in Escherichia coli L-forms.Communications biology · 2024Article
- Determining the rate-limiting processes for cell division in Escherichia coli.Nature communications · 2024Article
- In Vivo Cross-Linking Sheds Light on the Salmonella Divisome in Which PBP3 and PBP3Molecular microbiology · 2024Article
- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
- Article
- Role of the antiparallel double-stranded filament form of FtsA in activating thebioRxiv : the preprint server for biology · 2024Article
- Stay on track - revelations of bacterial cell wall synthesis enzymes and things that go by single-molecule imaging.Current opinion in microbiology · 2024Review
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Authors and funding
7 authors.
Funding
Abstract
The bacterial divisome is a macromolecular machine composed of more than 30 proteins that controls cell wall constriction during division. Here, we present a model of the structure and dynamics of the core complex of the E. coli divisome, supported by a combination of structure prediction, molecular dynamics simulation, single-molecule imaging, and mutagenesis. We focus on the septal cell wall synthase complex formed by FtsW and FtsI, and its regulators FtsQ, FtsL, FtsB, and FtsN. The results indicate extensive interactions in four regions in the periplasmic domains of the complex. FtsQ, FtsL, and FtsB support FtsI in an extended conformation, with the FtsI transpeptidase domain lifted away from the membrane through interactions among the C-terminal domains. FtsN binds between FtsI and FtsL in a region rich in residues with superfission (activating) and dominant negative (inhibitory) mutations. Mutagenesis experiments and simulations suggest that the essential domain of FtsN links FtsI and FtsL together, potentially modulating interactions between the anchor-loop of FtsI and the putative catalytic cavity of FtsW, thus suggesting a mechanism of how FtsN activates the cell wall synthesis activities of FtsW and FtsI.
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