EMD-35364

Single-particle
4.0 Å
EMD-35364 Deposition: 12/02/2023
Map released: 04/10/2023
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-35364

Cryo-EM structure of Mycobacterium tuberculosis ATP bound FtsEX/RipC complex in peptidisc

EMD-35364

Single-particle
4.0 Å
EMD-35364 Deposition: 12/02/2023
Map released: 04/10/2023
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
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
Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.
Li J , Xu X , Shi J, Hermoso JA , Sham LT , Luo M
(2023) Nat Commun , 14 , 7999 - 7999
PUBMED: 38044344
DOI: doi:10.1038/s41467-023-43770-6
ISSN: 2041-1723
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.