8X61
Cryo-EM structure of ATP-bound FtsE(E163Q)X
Summary for 8X61
| Entry DOI | 10.2210/pdb8x61/pdb |
| EMDB information | 38077 |
| Descriptor | Cell division ATP-binding protein FtsE, Cell division protein FtsX, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | abc transporter, cell division, transport protein |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 4 |
| Total formula weight | 127131.95 |
| Authors | Zhang, Z.Y.,Chen, Y.T. (deposition date: 2023-11-20, release date: 2024-05-08, Last modification date: 2025-07-16) |
| 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 (3.05 Å) |
Structure validation
Download full validation report
