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- Title
Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.
- Authors
Li, Jianwei; Xu, Xin; Shi, Jian; Hermoso, Juan A.; Sham, Lok-To; Luo, Min
- 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. Here, the authors use cryo-EM and biochemical approaches to characterise the structure and interactions of the FtsEX complex in Mycobacterium tuberculosis. The results show that FtsEX engages RipC in a unique way through a "Match and Fit" mechanism.
- Subjects
CELL division; CELLULAR control mechanisms; MYCOBACTERIUM tuberculosis; GRAM-positive bacteria; DRUG design; CELLULAR signal transduction
- Publication
Nature Communications, 2023, Vol 14, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-023-43770-6