8Y3X
Cell divisome sPG hydrolysis machinery FtsEX-EnvC
Summary for 8Y3X
Entry DOI | 10.2210/pdb8y3x/pdb |
EMDB information | 38906 |
Descriptor | Cell division ATP-binding protein FtsE, Cell division protein FtsX, Murein hydrolase activator EnvC, ... (4 entities in total) |
Functional Keywords | cell division, membrane protein |
Biological source | Escherichia coli More |
Total number of polymer chains | 5 |
Total formula weight | 173793.57 |
Authors | |
Primary citation | 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 Cited by 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: 38814940DOI: 10.1371/journal.pbio.3002628 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.11 Å) |
Structure validation
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