ArticleScientific reports2017
Structural analysis of variant of Helicobacter pylori MotB in its activated form, engineered as chimera of MotB and leucine zipper.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Biochemical characterization of paralyzed flagellum proteins A (PflA) and B (PflB) from Helicobacter pylori flagellar motor.Bioscience reports · 2024Article
- Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- The flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Periplasmic Domain of the Ion-Conducting Stator of Bacterial Flagella Regulates Force Generation.Frontiers in microbiology · 2022Review
- A new class of biological ion-driven rotary molecular motors with 5:2 symmetry.Frontiers in microbiology · 2022Review
- The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors.Frontiers in microbiology · 2021Review
- Living in a Foster Home: The Single Subpolar Flagellum Fla1 ofBiomolecules · 2020Review
- Evolution of the Stator Elements of Rotary Prokaryote Motors.Journal of bacteriology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotation of the bacterial flagellum is powered by a proton influx through the peptidoglycan (PG)-tethered stator ring MotA/B. MotA and MotB form an inner-membrane complex that does not conduct protons and does not bind to PG until it is inserted into the flagellar motor. The opening of the proton channel involves association of the plug helices in the periplasmic region of the MotB dimer into a parallel coiled coil. Here, we have characterised the structure of a soluble variant of full-length Helicobacter pylori MotB in which the plug helix was engineered to be locked in a parallel coiled coil state, mimicking the open state of the stator. Fluorescence resonance energy transfer measurements, combined with PG-binding assays and fitting of the crystal structures of MotB fragments to the small angle X-ray scattering (SAXS) data revealed that the protein's C-terminal domain has a PG-binding-competent conformation. Molecular modelling against the SAXS data suggested that the linker in H. pylori MotB forms a subdomain between the plug and the C-terminal domain, that 'clamps' the coiled coil of the plug, thus stabilising the activated form of the protein. Based on these results, we present a pseudo-atomic model structure of full-length MotB in its activated form.
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