Details

Autor(en) / Beteiligte

• Fujita, Junso
• Amesaka, Hiroshi
• Yoshizawa, Takuya
• Hibino, Kota
• Kamimura, Natsuki
• Kuroda, Natsuko
• Konishi, Takamoto
• Kato, Yuki
• Hara, Mizuho
• Inoue, Tsuyoshi
• Namba, Keiichi
• Tanaka, Shun-Ichi
• Matsumura, Hiroyoshi

Titel

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

Ist Teil von

• Nature communications, 2023-07, Vol.14 (1), p.4073-4073, Article 4073

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2023

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.