8IDC

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

Summary for 8IDC

• Entry DOI: 10.2210/pdb8idc/pdb
• EMDB information: 35363
• Descriptor: Cell division ATP-binding protein FtsE, NlpC/P60 family protein, Cell division protein FtsX (3 entities in total)
• Functional Keywords: complex, transport protein
• Biological source: Mycobacterium tuberculosis; More
• Total number of polymer chains: 5
• Total formula weight: 157029.02

Authors

Li, J.,Xu, X.,Luo, M. (deposition date: 2023-02-12, release date: 2023-10-04, Last modification date: 2024-10-30)

Primary citation

Li, J.,Xu, X.,Shi, J.,Hermoso, J.A.,Sham, L.T.,Luo, M.
Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.
Nat Commun, 14:7999-7999, 2023

PubMed 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.

PubMed: 38044344
DOI: 10.1038/s41467-023-43770-6

Experimental method

ELECTRON MICROSCOPY (3.9 Å)