8GZV

Klebsiella pneumoniae FtsZ complexed with monobody (P212121)

8GZV の概要

• エントリーDOI: 10.2210/pdb8gzv/pdb
• 分子名称: Cell division protein FtsZ, Monobody, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: cell division, monobody, gtpase, hydrolase, cell cycle
• 由来する生物種: Klebsiella pneumoniae; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42038.18

構造登録者

Matsumura, H.,Yoshizawa, T.,Fujita, J.,Tanaka, S.,Amesaka, H. (登録日: 2022-09-27, 公開日: 2023-07-19, 最終更新日: 2023-11-29)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)