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-Structure paper
タイトル | Structural insights into the FtsEX-EnvC complex regulation on septal peptidoglycan hydrolysis in Vibrio cholerae. |
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ジャーナル・号・ページ | Structure, Vol. 32, Issue 2, Page 188-199.e5, Year 2024 |
掲載日 | 2024年2月1日 |
著者 | Aili Hao / Yang Suo / Seok-Yong Lee / |
PubMed 要旨 | 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 ...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. |
リンク | Structure / PubMed:38070498 |
手法 | EM (単粒子) |
解像度 | 3.51 - 7.37 Å |
構造データ | EMDB-41760, PDB-8tzj: EMDB-41761, PDB-8tzk: EMDB-41762, PDB-8tzl: EMDB-41763: Cryo-EM structure of Vibrio cholerae FtsE Y20A mutant/FtsX/EnvC complex |
化合物 | ChemComp-MG: ChemComp-ADP: |
由来 |
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キーワード | TRANSPORT PROTEIN / membrane protein / enzyme |