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Showing 1–8 of 8 results
Advanced filters: Author: Randy B Stockbridge Clear advanced filters

  • Fluc-type channels—used by microorganisms to extrude toxic fluoride ions—have been suggested to adopt an unusual antiparallel topology across the membrane. Stockbridge et al.now provide the best evidence so far for this atypical arrangement, showing that specific monobodies block channel activity from both sides of the membrane.

    • Randy B. Stockbridge
    • Akiko Koide
    • Shohei Koide
    Research
    Nature Communications
    Volume: 5, P: 1-5

  • Eukaryotes, such as fungi, protozoa, and plants, resist fluoride using fluoride exporters called FEX. Here, authors determine a molecular structure of FEX from Candida albicans, and show that FEX is a single-pore, sodium-activated fluoride channel.

    • Chia-Yu Kang
    • Minjun An
    • Randy B. Stockbridge
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-13

  • Gdx-Clo is a bacterial transporter from the small multidrug resistance (SMR) family. Here, the authors use solid supported membrane electrophysiology to characterize Gdx-Clo functionally and report crystal structures of Gdx-Clo which confirm the dual topology architecture and offer insight into substrate binding and transport mechanism.

    • Ali A. Kermani
    • Christian B. Macdonald
    • Randy B. Stockbridge
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-9

  • Crystal structures of the CLCF proton-coupled fluoride antiporter Eca in two conformations capture two rotamers of the gating glutamate and reveal simultaneous accessibility of F– and H+ ions via separate pathways on opposite sides of the membrane.

    • Nicholas B. Last
    • Randy B. Stockbridge
    • Christopher Miller
    Research
    Nature Structural & Molecular Biology
    Volume: 25, P: 601-606

  • Protonation of periplasmic protein carboxylic groups creates a Donnan equilibrium in the bacterial periplasmic space at low pH, leading to accumulation of Cl− and unfolding and aggregation of periplasmic proteins, which can be rescued by chaperones.

    • Frederick Stull
    • Hannah Hipp
    • James C. A. Bardwell
    Research
    Nature Chemical Biology
    Volume: 14, P: 1051-1058

  • Microbial degradation and biosynthesis of fluorinated compounds is a field of increasing importance, but is hampered by the significant toxicity of fluoride. Here authors discuss emerging ideas on microbial defluorination/fluorination and fluoride resistance mechanisms, providing guidance on how this knowledge can guide future bioengineering approaches.

    • Randy B. Stockbridge
    • Lawrence P. Wackett
    ReviewsOpen Access
    Nature Communications
    Volume: 15, P: 1-12

  • Microorganisms can export toxic fluoride ions through highly selective channels of the Fluc family; here, the crystal structures of two bacterial Fluc homologues are presented, revealing that selectivity for small F− ions may arise from the proteins’ narrow pores and unusual anion coordination.

    • Randy B. Stockbridge
    • Ludmila Kolmakova-Partensky
    • Simon Newstead
    Research
    Nature
    Volume: 525, P: 548-551