9ISK
Cryo-EM structure of KpFtsZ-ZapA complex
Summary for 9ISK
| Entry DOI | 10.2210/pdb9isk/pdb |
| EMDB information | 60837 |
| Descriptor | Cell division protein FtsZ, Cell division protein ZapA, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, ... (5 entities in total) |
| Functional Keywords | bacterial cell division, divisome, ftsz, zapa, cell cycle |
| Biological source | Klebsiella pneumoniae subsp. pneumoniae MGH 78578 More |
| Total number of polymer chains | 14 |
| Total formula weight | 346659.53 |
| Authors | Fujita, J.,Hibino, K.,Kagoshima, G.,Kamimura, N.,Kato, Y.,Uehara, R.,Namba, K.,Uchihashi, T.,Matsumura, H. (deposition date: 2024-07-18, release date: 2025-07-23) |
| Primary citation | Fujita, J.,Kasai, K.,Hibino, K.,Kagoshima, G.,Kamimura, N.,Tobita, S.,Kato, Y.,Uehara, R.,Namba, K.,Uchihashi, T.,Matsumura, H. Structural basis for the interaction between the bacterial cell division proteins FtsZ and ZapA. Nat Commun, 16:5985-5985, 2025 Cited by PubMed Abstract: Cell division in most bacteria is regulated by the tubulin homolog FtsZ as well as ZapA, a FtsZ-associated protein. However, how FtsZ and ZapA function coordinately has remained elusive. Here we report the cryo-electron microscopy structure of the ZapA-FtsZ complex at 2.73 Å resolution. The complex forms an asymmetric ladder-like structure, in which the double antiparallel FtsZ protofilament on one side and a single protofilament on the other side are tethered by ZapA tetramers. In the complex, the extensive interactions of FtsZ with ZapA cause a structural change of the FtsZ protofilament, and the formation of the double FtsZ protofilament increases electrostatic repulsion. High-speed atomic force microscopy analysis revealed cooperative interactions of ZapA with FtsZ at a molecular level. Our findings not only provide a structural basis for the interaction between FtsZ and ZapA but also shed light on how ZapA binds to FtsZ protofilaments without disturbing FtsZ dynamics to promote cell division. PubMed: 40593603DOI: 10.1038/s41467-025-60940-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.73 Å) |
Structure validation
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