8TZL の概要
| エントリーDOI | 10.2210/pdb8tzl/pdb |
| EMDBエントリー | 41760 41761 41762 |
| 分子名称 | Cell division ATP-binding protein FtsE, Cell division protein FtsX, Peptidase M23, ... (5 entities in total) |
| 機能のキーワード | membrane protein, enzyme, transport protein |
| 由来する生物種 | Vibrio cholerae 詳細 |
| タンパク質・核酸の鎖数 | 5 |
| 化学式量合計 | 169112.79 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 38070498DOI: 10.1016/j.str.2023.11.007 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.55 Å) |
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