Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody

Junso Fujita, Hiroshi Amesaka, Takuya Yoshizawa, Kota Hibino, Natsuki Kamimura, Natsuko Kuroda, Takamoto Konishi, Yuki Kato, Mizuho Hara, Tsuyoshi Inoue, Keiichi Namba, Shun-ichi Tanaka () and Hiroyoshi Matsumura ()
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Junso Fujita: Osaka University
Hiroshi Amesaka: Kyoto Prefectural University
Takuya Yoshizawa: Ritsumeikan University
Kota Hibino: Ritsumeikan University
Natsuki Kamimura: Ritsumeikan University
Natsuko Kuroda: Ritsumeikan University
Takamoto Konishi: Ritsumeikan University
Yuki Kato: Ritsumeikan University
Mizuho Hara: Kyoto Prefectural University
Tsuyoshi Inoue: Osaka University
Keiichi Namba: Osaka University
Shun-ichi Tanaka: Kyoto Prefectural University
Hiroyoshi Matsumura: Ritsumeikan University

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: 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.

Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39807-5

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DOI: 10.1038/s41467-023-39807-5

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