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Showing 1–7 of 7 results
Advanced filters: Author: Ulf Diederichsen Clear advanced filters

  • Ground state destabilization is often evoked as a possible explanation of orotidine-5′-phosphate decarboxylase catalysis. Now, high-resolution structures of this enzyme provide time-resolved snapshots along its reaction coordinate revealing that transition-state stabilization by electrostatic interactions drives its reactivity.

    • Sören Rindfleisch
    • Matthias Krull
    • Kai Tittmann
    Research
    Nature Catalysis
    Volume: 5, P: 332-341

  • A NOS bridge between cysteine and lysine residues serves as an allosteric redox switch in the transaldolase enzyme of Neisseria gonorrhoeae, demonstrating the existence of protein regulatory switches that contain covalent crosslinks other than disulfides.

    • Marie Wensien
    • Fabian Rabe von Pappenheim
    • Kai Tittmann
    Research
    Nature
    Volume: 593, P: 460-464

  • Synaptotagmin-1 is known to accelerate membrane fusion during neuronal exocytosis in response to Ca2+, but how it does this is unclear. By probing the activity of synaptotagmin-1 under conditions of low ionic strength, it is now shown that SNARE-mediated fusion is dependent on synaptotagmin-1, which tethers liposomes together but at distances too far for fusion. Ca2+ then induces synaptotagmin-1 to bring the liposomes closer together, allowing fusion to proceed.

    • Geert van den Bogaart
    • Shashi Thutupalli
    • Reinhard Jahn
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 805-812

  • Clustering of proteins in the plasma membrane plays an important role in the regulation of both cellular signalling and membrane remodelling. Milovanovic et al.demonstrate that mismatch between transmembrane domain length and the lipid bilayer thickness is sufficient to drive clustering of SNARE proteins.

    • Dragomir Milovanovic
    • Alf Honigmann
    • Reinhard Jahn
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-10

  • Interactions between synaptotagmin-1 and the SNARE syntaxin-1 are known to mediate synaptic-vesicle exocytosis. Fusion experiments with artificial lipid membranes combined with the crystal structure of synaptotagmin's C2B domain bound to phosphoserine indicate that PIP2 clusters, organized by syntaxin, act as molecular beacons for vesicle docking and direct Ca2+-dependent membrane fusion.

    • Alf Honigmann
    • Geert van den Bogaart
    • Reinhard Jahn
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 679-686