8X61

Cryo-EM structure of ATP-bound FtsE(E163Q)X

8X61 の概要

• エントリーDOI: 10.2210/pdb8x61/pdb
• EMDBエントリー: 38077
• 分子名称: Cell division ATP-binding protein FtsE, Cell division protein FtsX, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: abc transporter, cell division, transport protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 127131.95

構造登録者

Zhang, Z.Y.,Chen, Y.T. (登録日: 2023-11-20, 公開日: 2024-05-08, 最終更新日: 2025-07-16)

主引用文献

Chen, Y.,Gu, J.,Yang, B.,Yang, L.,Pang, J.,Luo, Q.,Li, Y.,Li, D.,Deng, Z.,Dong, C.,Dong, H.,Zhang, Z.
Structure and activity of the septal peptidoglycan hydrolysis machinery crucial for bacterial cell division.
Plos Biol., 22:e3002628-e3002628, 2024

PubMed Abstract: The peptidoglycan (PG) layer is a critical component of the bacterial cell wall and serves as an important target for antibiotics in both gram-negative and gram-positive bacteria. The hydrolysis of septal PG (sPG) is a crucial step of bacterial cell division, facilitated by FtsEX through an amidase activation system. In this study, we present the cryo-EM structures of Escherichia coli FtsEX and FtsEX-EnvC in the ATP-bound state at resolutions of 3.05 Å and 3.11 Å, respectively. Our PG degradation assays in E. coli reveal that the ATP-bound conformation of FtsEX activates sPG hydrolysis of EnvC-AmiB, whereas EnvC-AmiB alone exhibits autoinhibition. Structural analyses indicate that ATP binding induces conformational changes in FtsEX-EnvC, leading to significant differences from the apo state. Furthermore, PG degradation assays of AmiB mutants confirm that the regulation of AmiB by FtsEX-EnvC is achieved through the interaction between EnvC-AmiB. These findings not only provide structural insight into the mechanism of sPG hydrolysis and bacterial cell division, but also have implications for the development of novel therapeutics targeting drug-resistant bacteria.

PubMed: 38814940
DOI: 10.1371/journal.pbio.3002628

実験手法

ELECTRON MICROSCOPY (3.05 Å)