ArticleNature communications2023
Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.
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 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Structural analysis of a Gram-positive type VII ABC transporter induced by cell wall-targeting antibiotics.Structure (London, England : 1993) · 2026Article
- Article
- Article
- Unique growth and morphology properties of Clade 5bioRxiv : the preprint server for biology · 2025Article
- The multiple roles of the NlpC_P60 peptidase family in mycobacteria - an underexplored target for antimicrobial drug discovery.FEBS letters · 2025Review
- Unique growth and morphology properties of Clade 5 Clostridioides difficile strains revealed by single-cell time-lapse microscopy.PLoS pathogens · 2025Article
- Modulation of the lytic apparatus by the FtsEX complex within the bacterial division machinery.FEBS letters · 2024Review
- Article
- DnaA modulates the gene expression and morphology of the Lyme disease spirochete.bioRxiv : the preprint server for biology · 2024Article
- Structure and activity of the septal peptidoglycan hydrolysis machinery crucial for bacterial cell division.PLoS biology · 2024Article
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6 authors.
Funding
Abstract
The FtsEX complex regulates, directly or via a protein mediator depending on bacterial genera, peptidoglycan degradation for cell division. In mycobacteria and Gram-positive bacteria, the FtsEX system directly activates peptidoglycan-hydrolases by a mechanism that remains unclear. Here we report our investigation of Mycobacterium tuberculosis FtsEX as a non-canonical regulator with high basal ATPase activity. The cryo-EM structures of the FtsEX system alone and in complex with RipC, as well as the ATP-activated state, unveil detailed information on the signal transduction mechanism, leading to the activation of RipC. Our findings indicate that RipC is recognized through a "Match and Fit" mechanism, resulting in an asymmetric rearrangement of the extracellular domains of FtsX and a unique inclined binding mode of RipC. This study provides insights into the molecular mechanisms of FtsEX and RipC regulation in the context of a critical human pathogen, guiding the design of drugs targeting peptidoglycan remodeling.
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