ArticleNature microbiology2023
Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL.
Article in Nature microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- Altered regulation of septal peptidoglycan synthesis modulates β-lactam susceptibility in Pseudomonas aeruginosa.PLoS genetics · 2026Article
- Structure and Membrane Interactions of Two Helices from Mycobacterium tuberculosis FtsL, One Transmembrane and One Amphipathic.Journal of the American Chemical Society · 2026Article
- Detection of Protein-Protein Interactions in Escherichia coli With Single Molecule Sensitivity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Article
- FtsW protein-protein interactions visualized in live Staphylococcus aureus cells by FLIM-FRET.Nature communications · 2026Article
- In Silico Druggability Assessment ofAntibiotics (Basel, Switzerland) · 2026Article
- Antibacterial Benzimidazole-2-Methanamines as Allosteric Modulators ofJournal of medicinal chemistry · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 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
- Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular dissection of Class A PBP function uncovers novel features of the non-canonical Clostridioides difficile divisome complex.PLoS genetics · 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
- Mechanism of lateral cell-wall expansion at a constant diameter in Bacillus subtilis.Nature communications · 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
- SpoIIE drives asymmetric cell division inbioRxiv : the preprint server for biology · 2025Article
- Third track model for coordination of septal peptidoglycan synthesis and degradation by FtsN in Escherichia coli.Nature microbiology · 2025Article
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6 authors.
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Abstract
In most bacteria, cell division relies on the synthesis of new cell wall material by the multiprotein divisome complex. Thus, at the core of the divisome are the transglycosylase FtsW, which synthesises peptidoglycan strands from its substrate Lipid II, and the transpeptidase FtsI that cross-links these strands to form a mesh, shaping and protecting the bacterial cell. The FtsQ-FtsB-FtsL trimeric complex interacts with the FtsWI complex and is involved in regulating its enzymatic activities; however, the structure of this pentameric complex is unknown. Here, we present the cryogenic electron microscopy structure of the FtsWIQBL complex from Pseudomonas aeruginosa at 3.7 Å resolution. Our work reveals intricate structural details, including an extended coiled coil formed by FtsL and FtsB and the periplasmic interaction site between FtsL and FtsI. Our structure explains the consequences of previously reported mutations and we postulate a possible activation mechanism involving a large conformational change in the periplasmic domain. As FtsWIQBL is central to the divisome, our structure is foundational for the design of future experiments elucidating the precise mechanism of bacterial cell division, an important antibiotic target.
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