ArticleProceedings of the National Academy of Sciences of the United States of America2015
β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Bactofilins are essential spatial organizers of peptidoglycan insertion in the Lyme disease spirocheteJournal of bacteriology · 2026Article
- Collecting Large Datasets of Unambiguous Structural Restraints for Protein Structure Determination by 4D Proton-Detected Solid-State NMR.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Atomic-level architecture and assembly mechanism of high-order structures of RIPK1 fibril revealed by integrated structural biology.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- Polymerization and flanking domains of the bactofilin BacA collectively regulate stalk formation in Asticcacaulis biprosthecum.PLoS genetics · 2025Article
- Functional specialization of the subdomains of a bactofilin driving stalk morphogenesis inbioRxiv : the preprint server for biology · 2024Article
- Halofilins as emerging bactofilin families of archaeal cell shape plasticity orchestrators.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A dynamic bactofilin cytoskeleton cooperates with an M23 endopeptidase to control bacterial morphogenesis.eLife · 2024Article
- VirB, a key transcriptional regulator ofmBio · 2023Article
- VirB, a key transcriptional regulator ofbioRxiv : the preprint server for biology · 2023Article
- Interacting bactofilins impact cell shape of the MreB-less multicellular Rhodomicrobium vannielii.PLoS genetics · 2023Article
- Accurate Determination of Motional Amplitudes in Biomolecules by Solid-State NMR.ACS physical chemistry Au · 2023Article
- Distinct regions ofeLife · 2022Article
- From Angstroms to Nanometers: Measuring Interatomic Distances by Solid-State NMR.Chemical reviews · 2022Review
- Insights Into the Helical Shape Complex ofFrontiers in microbiology · 2022Article
- A Dynamic, Ring-Forming Bactofilin Critical for Maintaining Cell Size in the Obligate Intracellular Bacterium Chlamydia trachomatis.Infection and immunity · 2021Article
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- A Division of Labor in the Recruitment and Topological Organization of a Bacterial Morphogenic Complex.Current biology : CB · 2020Article
- Prediction of fibril formation by early-stage amyloid peptide aggregation.Journal of pharmaceutical analysis · 2020Article
- Cell morphology as a virulence determinant: lessons from Helicobacter pylori.Current opinion in microbiology · 2020Review
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bactofilins are a widespread class of bacterial filament-forming proteins, which serve as cytoskeletal scaffolds in various cellular pathways. They are characterized by a conserved architecture, featuring a central conserved domain (DUF583) that is flanked by variable terminal regions. Here, we present a detailed investigation of bactofilin filaments from Caulobacter crescentus by high-resolution solid-state NMR spectroscopy. De novo sequential resonance assignments were obtained for residues Ala39 to Phe137, spanning the conserved DUF583 domain. Analysis of the secondary chemical shifts shows that this core region adopts predominantly β-sheet secondary structure. Mutational studies of conserved hydrophobic residues located in the identified β-strand segments suggest that bactofilin folding and polymerization is mediated by an extensive and redundant network of hydrophobic interactions, consistent with the high intrinsic stability of bactofilin polymers. Transmission electron microscopy revealed a propensity of bactofilin to form filament bundles as well as sheet-like, 2D crystalline assemblies, which may represent the supramolecular arrangement of bactofilin in the native context. Based on the diffraction pattern of these 2D crystalline assemblies, scanning transmission electron microscopy measurements of the mass per length of BacA filaments, and the distribution of β-strand segments identified by solid-state NMR, we propose that the DUF583 domain adopts a β-helical architecture, in which 18 β-strand segments are arranged in six consecutive windings of a β-helix.
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