ArticlePLoS biology2022
FtsZ filament structures in different nucleotide states reveal the mechanism of assembly dynamics.
Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Computationally Generated Plant-Derived Berberine-Based Hybrid Compounds as Potential Dual Binders toInternational journal of molecular sciences · 2026Article
- Pharmacophore-based virtual screening, molecular docking, MD simulation, MM-GBSA energy calculation and DFT analysis for theRSC advances · 2026Article
- Distinct filament morphology and membrane tethering features of the dual FtsZ paralogs in Odinarchaeota.The EMBO journal · 2025Article
- A FtsZ cis disassembly element acts in Z-ring assembly during bacterial cell division.Nature communications · 2025Article
- Exploring the structural and dynamical features of bacterial-tubulin FtsZ.Biophysical journal · 2025Article
- Complex state transitions of the bacterial cell division protein FtsZ.Molecular biology of the cell · 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
- Self-organization of mortal filaments and its role in bacterial division ring formation.Nature physics · 2024Article
- Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody.Nature communications · 2023Article
- Filamentous temperature sensitive mutant Z: a putative target to combat antibacterial resistance.RSC advances · 2023Review
- Article
- The Search for Antibacterial Inhibitors Targeting Cell Division Protein FtsZ at Its Nucleotide and Allosteric Binding Sites.Biomedicines · 2022Review
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Treadmilling protein filaments perform essential cellular functions by growing from one end while shrinking from the other, driven by nucleotide hydrolysis. Bacterial cell division relies on the primitive tubulin homolog FtsZ, a target for antibiotic discovery that assembles into single treadmilling filaments that hydrolyse GTP at an active site formed upon subunit association. We determined high-resolution filament structures of FtsZ from the pathogen Staphylococcus aureus in complex with different nucleotide analogs and cations, including mimetics of the ground and transition states of catalysis. Together with mutational and biochemical analyses, our structures reveal interactions made by the GTP γ-phosphate and Mg2+ at the subunit interface, a K+ ion stabilizing loop T7 for co-catalysis, new roles of key residues at the active site and a nearby crosstalk area, and rearrangements of a dynamic water shell bridging adjacent subunits upon GTP hydrolysis. We propose a mechanistic model that integrates nucleotide hydrolysis signaling with assembly-associated conformational changes and filament treadmilling. Equivalent assembly mechanisms may apply to more complex tubulin and actin cytomotive filaments that share analogous features with FtsZ.
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