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TitleStructural insights into the FtsEX-EnvC complex regulation on septal peptidoglycan hydrolysis in Vibrio cholerae.
Journal, issue, pagesStructure, Vol. 32, Issue 2, Page 188-199.e5, Year 2024
Publish dateFeb 1, 2024
AuthorsAili Hao / Yang Suo / Seok-Yong Lee /
PubMed AbstractDuring 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 ...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.
External linksStructure / PubMed:38070498
MethodsEM (single particle)
Resolution3.51 - 7.37 Å
Structure data

41760

8tzj

EMDB-41760, PDB-8tzj:
Cryo-EM structure of Vibrio cholerae FtsE/FtsX complex
Method: EM (single particle) / Resolution: 3.51 Å

41761

8tzk

EMDB-41761, PDB-8tzk:
Cryo-EM structure of Vibrio cholerae FtsE/FtsX/EnvC complex, shortened
Method: EM (single particle) / Resolution: 3.55 Å

41762

8tzl

EMDB-41762, PDB-8tzl:
Cryo-EM structure of Vibrio cholerae FtsE/FtsX/EnvC complex, full-length
Method: EM (single particle) / Resolution: 3.55 Å

EMDB-41763: Cryo-EM structure of Vibrio cholerae FtsE Y20A mutant/FtsX/EnvC complex
Method: EM (single particle) / Resolution: 7.37 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • vibrio cholerae (bacteria)
KeywordsTRANSPORT PROTEIN / membrane protein / enzyme

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