ArticleActa crystallographica. Section F, Structural biology communications2020
High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.
Article in Acta crystallographica. Section F, Structural biology communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- Bacterial cell division protein FtsZ complexes with a phage protein to activate bacterial immunity.Nature microbiology · 2026Article
- Optimizing spatial organization of FtsZ rings for large-scale constriction in synthetic cells.Nature communications · 2026Article
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- FtsZ as a novel target for antibiotics development: Promises and challenges.Acta pharmaceutica Sinica. B · 2025Review
- A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division.Nature communications · 2025Article
- High-throughput discovery of inhibitory protein fragments with AlphaFold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Complex state transitions of the bacterial cell division protein FtsZ.Molecular biology of the cell · 2024Article
- High-throughput discovery of inhibitory protein fragments with AlphaFold.bioRxiv : the preprint server for biology · 2024Article
- Computational docking of FtsZ: Survey of promising antibiotic compounds.Biochemistry and biophysics reports · 2024Article
- Molecular dynamics simulations reveal differences in the conformational stability of FtsZs derived from Staphylococcus aureus and Bacillus subtilis.Scientific reports · 2024Article
- Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody.Nature communications · 2023Article
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- Properties of Configurationally Stable Atropoenantiomers in Macrocyclic Natural Products and the Chrysophaentin Family.Accounts of chemical research · 2023Review
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- Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Mapping functional regions of essential bacterial proteins with dominant-negative protein fragments.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- FtsZ filament structures in different nucleotide states reveal the mechanism of assembly dynamics.PLoS biology · 2022Article
- How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?Frontiers in microbiology · 2022Review
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadmilling involves a switch from a relaxed (R) state, favored for monomers, to a tense (T) conformation, which is favored upon association into filaments. The R conformation has been observed in numerous monomeric FtsZ crystal structures and the T conformation in Staphylococcus aureus FtsZ crystallized as assembled filaments. However, while Escherichia coli has served as a main model system for the study of the Z-ring and the associated divisome, a structure has not yet been reported for E. coli FtsZ. To address this gap, structures were determined of the E. coli FtsZ mutant FtsZ(L178E) with GDP and GTP bound to 1.35 and 1.40 Å resolution, respectively. The E. coli FtsZ(L178E) structures both crystallized as straight filaments with subunits in the R conformation. These high-resolution structures can be employed to facilitate experimental cell-division studies and their interpretation in E. coli.
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