8GZW
Klebsiella pneumoniae FtsZ complexed with monobody (P21)
Summary for 8GZW
| Entry DOI | 10.2210/pdb8gzw/pdb |
| Descriptor | Cell division protein FtsZ, Monobody, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | cell division, monobody, gtpase, hydrolase, cell cycle |
| Biological source | Klebsiella pneumoniae More |
| Total number of polymer chains | 6 |
| Total formula weight | 126114.54 |
| Authors | Matsumura, H.,Yoshizawa, T.,Fujita, J.,Tanaka, S.,Amesaka, H. (deposition date: 2022-09-27, release date: 2023-07-19, Last modification date: 2023-11-29) |
| Primary citation | Fujita, J.,Amesaka, H.,Yoshizawa, T.,Hibino, K.,Kamimura, N.,Kuroda, N.,Konishi, T.,Kato, Y.,Hara, M.,Inoue, T.,Namba, K.,Tanaka, S.I.,Matsumura, H. Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody. Nat Commun, 14:4073-4073, 2023 Cited by PubMed Abstract: FtsZ polymerizes into protofilaments to form the Z-ring that acts as a scaffold for accessory proteins during cell division. Structures of FtsZ have been previously solved, but detailed mechanistic insights are lacking. Here, we determine the cryoEM structure of a single protofilament of FtsZ from Klebsiella pneumoniae (KpFtsZ) in a polymerization-preferred conformation. We also develop a monobody (Mb) that binds to KpFtsZ and FtsZ from Escherichia coli without affecting their GTPase activity. Crystal structures of the FtsZ-Mb complexes reveal the Mb binding mode, while addition of Mb in vivo inhibits cell division. A cryoEM structure of a double-helical tube of KpFtsZ-Mb at 2.7 Å resolution shows two parallel protofilaments. Our present study highlights the physiological roles of the conformational changes of FtsZ in treadmilling that regulate cell division. PubMed: 37429870DOI: 10.1038/s41467-023-39807-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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