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Showing 1–10 of 10 results
Advanced filters: Author: Inga Hänelt Clear advanced filters

  • Archaeal glutamate transporter homologs catalyze the coupled uptake of aspartate and sodium ions. A new crystal structure of GltTk from Thermococcus kodakarensis shows the empty transporter oriented in the outward-facing conformation after substrate delivery, revealing how it is reset in preparation for another translocation cycle.

    • Sonja Jensen
    • Albert Guskov
    • Dirk Jan Slotboom
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1224-1226

  • GltPh is a homotrimeric Na+-coupled aspartate transporter that belongs to the glutamate transporter family. The conformational changes that occur during GltPh transport are now directly observed using EPR spectroscopy, revealing that the transporting domains sample multiple states, regardless of the presence of substrate or ions.

    • Inga Hänelt
    • Dorith Wunnicke
    • Dirk Jan Slotboom
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 210-214

  • KdpFABC is a high-affinity bacterial K+ pump which combines the ion channel-like KdpA and the P-type ATPase KdpB. Here, the authors elucidate the mechanisms underlying transport and the coupling to ATP hydrolysis, and provide evidence that ions are transported via an intersubunit tunnel through KdpA and KdpB.

    • Jakob M. Silberberg
    • Robin A. Corey
    • Inga Hänelt
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • KUP transporters facilitate potassium uptake by the co-transport of protons and are key players in potassium homeostasis. Here authors identify the potassium importer KimA from Bacillus subtilis as a new member of the KUP transporter family and show the cryo-EM structure of KimA in an inward-occluded, trans-inhibited conformation.

    • Igor Tascón
    • Joana S. Sousa
    • Inga Hänelt
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • Cells maintain membrane fluidity by regulating lipid saturation, but the molecular mechanisms of this homeoviscous adaptation remain poorly understood. Here authors reconstituted the core machinery for regulating lipid saturation in baker’s yeast to directly characterize its response to defined membrane environments and uncover its mode-of-action.

    • Stephanie Ballweg
    • Erdinc Sezgin
    • Robert Ernst
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • Glutamate transporters are integral membrane proteins that facilitate neurotransmitter uptake from the synaptic cleft into the cytoplasm of glial cells and neurons, the mechanism of transport involves transitions between extracellular- and intracellular-facing conformations; here the authors used single-molecule fluorescence resonance energy transfer imaging to directly observe conformational dynamics in trimers of a bacterial homologue of glutamate transporters that was embedded in the membrane.

    • Guus B. Erkens
    • Inga Hänelt
    • Antoine M. van Oijen
    Research
    Nature
    Volume: 502, P: 119-123