8TZL

Cryo-EM structure of Vibrio cholerae FtsE/FtsX/EnvC complex, full-length

This is a non-PDB format compatible entry.

Summary for 8TZL

• Entry DOI: 10.2210/pdb8tzl/pdb
• EMDB information: 41760 41761 41762
• Descriptor: Cell division ATP-binding protein FtsE, Cell division protein FtsX, Peptidase M23, ... (5 entities in total)
• Functional Keywords: membrane protein, enzyme, transport protein
• Biological source: Vibrio cholerae; More
• Total number of polymer chains: 5
• Total formula weight: 169112.79

Authors

Hao, A.,Lee, S.-Y. (deposition date: 2023-08-27, release date: 2023-12-20, Last modification date: 2024-02-14)

Primary citation

Hao, A.,Suo, Y.,Lee, S.Y.
Structural insights into the FtsEX-EnvC complex regulation on septal peptidoglycan hydrolysis in Vibrio cholerae.
Structure, 32:188-199.e5, 2024

PubMed Abstract: During bacterial cell division, hydrolysis of septal peptidoglycan (sPG) is crucial for cell separation. This sPG hydrolysis is performed by the enzyme amidases whose activity is regulated by the integral membrane protein complex FtsEX-EnvC. FtsEX is an ATP-binding cassette transporter, and EnvC is a long coiled-coil protein that interacts with and activates the amidases. The molecular mechanism by which the FtsEX-EnvC complex activates amidases remains largely unclear. We present the cryo-electron microscopy structure of the FtsEX-EnvC complex from the pathogenic bacteria V. cholerae (FtsEX-EnvC). FtsEX-EnvC in the presence of ADP adopts a distinct conformation where EnvC is "horizontally extended" rather than "vertically extended". Subsequent structural studies suggest that EnvC can swing between these conformations in space in a nucleotide-dependent manner. Our structural analysis and functional studies suggest that FtsEX-EnvC employs spatial control of EnvC for amidase activation, providing mechanistic insights into the FtsEX-EnvC regulation on septal peptidoglycan hydrolysis.

PubMed: 38070498
DOI: 10.1016/j.str.2023.11.007

Experimental method

ELECTRON MICROSCOPY (3.55 Å)