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Showing 1–7 of 7 results
Advanced filters: Author: Gerard Huysmans Clear advanced filters

  • This study reveals the mechanism by which protons gate a CLC-type Cl−/H+ exchanger. The authors show that pH-dependent concerted structural rearrangements open the H+ pathway, which allosterically enables the Cl− pore opening and ion exchange.

    • Eva Fortea
    • Sangyun Lee
    • Alessio Accardi
    Research
    Nature Structural & Molecular Biology
    Volume: 31, P: 644-656

  • Excitatory amino acid transporters (EAATs) are crucial for the removal of excitatory amino acids from the synaptic cleft. Here authors combined high-speed atomic force microscopy line-scanning with automated state assignment for the determination of transport dynamics of GltPh, a prokaryotic EAAT homologue, with millisecond temporal resolution.

    • Tina R. Matin
    • George R. Heath
    • Simon Scheuring
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Bacterial autotransporters are folded in a process that entraps segments of their N-terminal passenger domain. Here, Leyton et al. identify glycine-aromatic mortise and tenon motifs that mediate the passenger domain’s translocation to the bacterial cell surface, and show that the motifs are evolutionarily conserved.

    • Denisse L. Leyton
    • Matthew D. Johnson
    • Trevor Lithgow
    Research
    Nature Communications
    Volume: 5, P: 1-11

  • Autotransporter passenger domains are presented on or released from the bacterial surface upon translocation through an outer membrane β-barrel anchor. Here the authors study the two E. coli autotransporters Pet and EspP and propose that the β-barrel anchor acts as a vector to nucleate the folding of the passenger domain.

    • Xiaojun Yuan
    • Matthew D. Johnson
    • Denisse L. Leyton
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-12