8IBN
Cryo-EM structure of KpFtsZ single filament
Summary for 8IBN
Entry DOI | 10.2210/pdb8ibn/pdb |
Related | 8GZV 8GZW 8GZX 8GZY 8H1O |
EMDB information | 34429 35344 |
Descriptor | Cell division protein FtsZ, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, POTASSIUM ION (3 entities in total) |
Functional Keywords | bacterial cell division, divisome, monobody, cell cycle |
Biological source | Klebsiella pneumoniae |
Total number of polymer chains | 4 |
Total formula weight | 164540.93 |
Authors | Fujita, J.,Amesaka, H.,Yoshizawa, T.,Kuroda, N.,Kamimura, N.,Hibino, K.,Konishi, T.,Kato, Y.,Hara, M.,Inoue, T.,Namba, K.,Tanaka, S.,Matsumura, H. (deposition date: 2023-02-10, release date: 2023-08-02, Last modification date: 2024-05-08) |
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 | ELECTRON MICROSCOPY (3.03 Å) |
Structure validation
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