ArticleThe Journal of biological chemistry2014
Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Coiled-coil homo-oligomerization and disaggregase Hsp104 act in parallel to stabilize orphan septins.bioRxiv : the preprint server for biology · 2026Article
- Ubiquitin-derived artificial binding proteins targeting oncofetal fibronectin reveal scaffold plasticity by β-strand slippage.Communications biology · 2024Article
- Evolutionary degeneration of septins into pseudoGTPases: impacts on a hetero-oligomeric assembly interface.Frontiers in cell and developmental biology · 2023Article
- Article
- The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021Review
- Article
- Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILRα immune cell receptor.The Journal of biological chemistry · 2017Article
- Septin structure and filament assembly.Biophysical reviews · 2017Review
- Filaments and fingers: Novel structural aspects of the single septin fromThe Journal of biological chemistry · 2017Article
- Article
- High pressureJournal of biomolecular NMR · 2017Article
- The Mammalian Septin Interactome.Frontiers in cell and developmental biology · 2017Review
- Effects of Bni5 Binding on Septin Filament Organization.Journal of molecular biology · 2016Article
- Septin Mutations in Human Cancers.Frontiers in cell and developmental biology · 2016Review
- A FRET-based method for monitoring septin polymerization and binding of septin-associated proteins.Methods in cell biology · 2016Article
- A Förster Resonance Energy Transfer (FRET)-based System Provides Insight into the Ordered Assembly of Yeast Septin Hetero-octamers.The Journal of biological chemistry · 2015Article
- Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis.The EMBO journal · 2015Article
- Lean forward: Genetic analysis of temperature-sensitive mutants unfolds the secrets of oligomeric protein complex assembly.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014Article
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10 authors.
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Abstract
Septins are filament-forming GTP-binding proteins involved in important cellular events, such as cytokinesis, barrier formation, and membrane remodeling. Here, we present two crystal structures of the GTPase domain of a Schistosoma mansoni septin (SmSEPT10), one bound to GDP and the other to GTP. The structures have been solved at an unprecedented resolution for septins (1.93 and 2.1 Å, respectively), which has allowed for unambiguous structural assignment of regions previously poorly defined. Consequently, we provide a reliable model for functional interpretation and a solid foundation for future structural studies. Upon comparing the two complexes, we observe for the first time the phenomenon of a strand slippage in septins. Such slippage generates a front-back communication mechanism between the G and NC interfaces. These data provide a novel mechanistic framework for the influence of nucleotide binding to the GTPase domain, opening new possibilities for the study of the dynamics of septin filaments.
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