EMD-35364
Cryo-EM structure of Mycobacterium tuberculosis ATP bound FtsEX/RipC complex in peptidisc
EMD-35364
Single-particle4.0 Å
![EMD-35364](https://www.ebi.ac.uk/emdb/images/entry/EMD-35364/400_35364.gif)
Map released: 04/10/2023
Last modified: 23/10/2024
Sample Organism:
Mycobacterium tuberculosis
Sample: complex of FtsEX-RipC-ATP
Fitted models: 8idd (Avg. Q-score: 0.309)
Deposition Authors: Li J
,
Xu X
,
Luo M
Sample: complex of FtsEX-RipC-ATP
Fitted models: 8idd (Avg. Q-score: 0.309)
Deposition Authors: Li J
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![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
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Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.
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.
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.