EMD-35344

Helical reconstruction
3.03 Å
EMD-35344 Deposition: 10/02/2023
Map released: 02/08/2023
Last modified: 08/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-35344

Cryo-EM structure of KpFtsZ single filament

EMD-35344

Helical reconstruction
3.03 Å
EMD-35344 Deposition: 10/02/2023
Map released: 02/08/2023
Last modified: 08/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Klebsiella pneumoniae
Sample: Cryo-EM structure of KpFtsZ single filament
Fitted models: 8ibn (Avg. Q-score: 0.36)
Raw data: EMPIAR-11426

Deposition 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
Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody.
PUBMED: 37429870
DOI: doi:10.1038/s41467-023-39807-5
ISSN: 2041-1723
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.