8H1O

Cryo-EM structure of KpFtsZ-monobody double helical tube

Summary for 8H1O

• Entry DOI: 10.2210/pdb8h1o/pdb
• Related: 8GZV 8GZW 8GZX 8GZY
• EMDB information: 34429
• Descriptor: Cell division protein FtsZ, Mb(Ec/KpFtsZ_S1), GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: bacterial cell division, divisome, ftsz, monobody, tubulin, cell cycle
• Biological source: Klebsiella pneumoniae; More
• Total number of polymer chains: 2
• Total formula weight: 50800.00

Authors

Fujita, J.,Amesaka, H.,Yoshizawa, T.,Kuroda, N.,Kamimura, N.,Hara, M.,Inoue, T.,Namba, K.,Tanaka, S.,Matsumura, H. (deposition date: 2022-10-03, release date: 2023-08-02, Last modification date: 2024-07-03)

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

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: 37429870
DOI: 10.1038/s41467-023-39807-5

Experimental method

ELECTRON MICROSCOPY (2.67 Å)