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Showing 1–11 of 11 results
Advanced filters: Author: Oleg Sitsel Clear advanced filters

  • A genome-wide CRISPR–Cas9-mediated knockout screen in Drosophila cells identifies Visgun as a proteinaceous receptor for toxin complex toxins, demonstrating the utility of this approach for investigating insecticidal toxins and pathogens.

    • Ying Xu
    • Raghuvir Viswanatha
    • Min Dong
    Research
    Nature
    Volume: 610, P: 349-355

  • The X-ray crystal structures of a zinc-ion-transporting P-type ATPase are solved in a zinc-free, phosphoenzyme ‘ground’ state and in a transition state of dephosphorylation, characterizing these transporters of an essential micronutrient that is needed for many biological processes but is cytotoxic when free.

    • Kaituo Wang
    • Oleg Sitsel
    • Pontus Gourdon
    Research
    Nature
    Volume: 514, P: 518-522

  • Although Tc toxins are a major class of bacterial toxin translocation systems, little is known about their receptor binding. Here, the authors identify heparins/heparan sulfates and Lewis antigens as receptors for different Tc toxins, determine cryo-EM structures of three toxin-glycan complexes and propose a two-step cell adhesion mechanism for Tc toxins.

    • Daniel Roderer
    • Felix Bröcker
    • Stefan Raunser
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • Tc toxins are a major class of bacterial toxin translocation systems that inject toxic enzymes into target cells. Here the authors present functional and structural data showing that the toxic enzyme can be replaced by other small proteins and identify prerequisites required for successful translocation, which could facilitate the development of functional Tc-based protein injection devices.

    • Daniel Roderer
    • Evelyn Schubert
    • Stefan Raunser
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-11

  • Most compounds form crystals so small that scientists cannot experimentally determine their atomic structures using X-ray crystallography. Microcrystal electron diffraction now provides a unique solution for this challenge.

    • Oleg Sitsel
    • Stefan Raunser
    News & Views
    Nature Chemistry
    Volume: 11, P: 106-108

  • P-type ATPases adopt different conformations during their transport cycle, including autophosphorylated forms. The structure of type IB P-type ATPase CopA is now solved in its E2P state. Comparison with a previous E2Pi structure indicates that dephosphorylation is not coupled to ion extrusion, in contrast to mechanisms in type IIA SERCA. The findings explain the effect of disease-related mutations in human Cu+ transporters.

    • Magnus Andersson
    • Daniel Mattle
    • Pontus Gourdon
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 43-48

  • Thorsten Wagner et al. present SPHIRE-crYOLO, a particle picking software for selecting particles from digital micrographs in cryoEM data. After training, the method automatically recognizes particles with high recall and precision, simplifying data pre-processing.

    • Thorsten Wagner
    • Felipe Merino
    • Stefan Raunser
    ResearchOpen Access
    Communications Biology
    Volume: 2, P: 1-13