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- W4302282022 abstract "Abstract FtsZ, a bacterial tubulin homologue, forms protofilaments and the Z-ring, which acts as a scaffold for accessory proteins during cell division. Although various studies have revealed its molecular mechanisms, the lack of high-resolution solution structures has hindered the understanding of the detailed mechanisms. Here, we developed a monobody (Mb) that binds FtsZs from Escherichia coli and Klebsiella pneumoniae (KpFtsZ) without affecting their GTPase activities. When expressed in E. coli cells, the Mb did not inhibit Z-ring formation but did inhibit cell division. The crystal structures of the KpFtsZ–Mb complexes revealed the epitope, and the cryoEM structure at 2.67 Å resolution showed a double helical tube consisting of two KpFtsZ protofilaments stabilized by the Mb filling interfilament gaps. Our structural analyses highlight the similarity between the microtubule and the FtsZ tube and the importance of the plasticity of FtsZ protofilaments." @default.
- W4302282022 created "2022-10-06" @default.
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- W4302282022 date "2022-10-05" @default.
- W4302282022 modified "2023-10-01" @default.
- W4302282022 title "High-resolution structure of a microtubule-like tube composed of FtsZ–monobody complexes" @default.
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- W4302282022 doi "https://doi.org/10.1101/2022.10.05.510932" @default.
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