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  1. Article

    Open Access

    Yersinia entomophaga Tc toxin is released by T10SS-dependent lysis of specialized cell subpopulations

    Disease-causing bacteria secrete numerous toxins to invade and subjugate their hosts. Unlike many smaller toxins, the secretion machinery of most large toxins remains enigmatic. By combining genomic editing, p...

    Oleg Sitsel, Zhexin Wang, Petra Janning, Lara Kroczek in Nature Microbiology (2024)

  2. Article

    Open Access

    Molecular basis for selective uptake and elimination of organic anions in the kidney by OAT1

    In mammals, the kidney plays an essential role in maintaining blood homeostasis through the selective uptake, retention or elimination of toxins, drugs and metabolites. Organic anion transporters (OATs) are re...

    Joanne L. Parker, Takafumi Kato, Gabriel Kuteyi in Nature Structural & Molecular Biology (2023)

  3. Article

    Open Access

    TomoTwin: generalized 3D localization of macromolecules in cryo-electron tomograms with structural data mining

    Cryogenic-electron tomography enables the visualization of cellular environments in extreme detail, however, tools to analyze the full amount of information contained within these densely packed volumes are st...

    Gavin Rice, Thorsten Wagner, Markus Stabrin, Oleg Sitsel, Daniel Prumbaum in Nature Methods (2023)

  4. No Access

    Article

    CRISPR screens in Drosophila cells identify Vsg as a Tc toxin receptor

    Entomopathogenic nematodes are widely used as biopesticides1,2. Their insecticidal activity depends on symbiotic bacteria such as Photorhabdus luminescens, which produces toxin complex (Tc) toxins as major virule...

    Ying Xu, Raghuvir Viswanatha, Oleg Sitsel, Daniel Roderer, Haifang Zhao in Nature (2022)

  5. Article

    Open Access

    Glycan-dependent cell adhesion mechanism of Tc toxins

    Toxin complex (Tc) toxins are virulence factors of pathogenic bacteria. Tcs are composed of three subunits: TcA, TcB and TcC. TcA facilitates receptor–toxin interaction and membrane permeation, TcB and TcC for...

    Daniel Roderer, Felix Bröcker, Oleg Sitsel, Paulina Kaplonek in Nature Communications (2020)

  6. Article

    Open Access

    Towards the application of Tc toxins as a universal protein translocation system

    Tc toxins are bacterial protein complexes that inject cytotoxic enzymes into target cells using a syringe-like mechanism. Tc toxins are composed of a membrane translocator and a cocoon that encapsulates a toxi...

    Daniel Roderer, Evelyn Schubert, Oleg Sitsel, Stefan Raunser in Nature Communications (2019)

  7. Article

    Open Access

    SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM

    Selecting particles from digital micrographs is an essential step in single-particle electron cryomicroscopy (cryo-EM). As manual selection of complete datasets—typically comprising thousands of particles—is a...

    Thorsten Wagner, Felipe Merino, Markus Stabrin, Toshio Moriya in Communications Biology (2019)

  8. No Access

    Article

    Big insights from tiny crystals

    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 t...

    Oleg Sitsel, Stefan Raunser in Nature Chemistry (2019)

  9. No Access

    Protocol

    Overproduction of PIB-Type ATPases

    Understanding of the functions and mechanisms of fundamental processes in the cell requires structural information. Structural studies of membrane proteins typically necessitate large amounts of purified and p...

    **angyu Liu, Oleg Sitsel, Kaituo Wang, Pontus Gourdon in P-Type ATPases (2016)

  10. No Access

    Protocol

    Crystallization of P-type ATPases by the High Lipid–Detergent (HiLiDe) Method

    Determining structures of membrane proteins remains a significant challenge. A technique utilizing high lipid–detergent concentrations (“HiLiDe”) circumvents the major bottlenecks of current membrane protein c...

    Oleg Sitsel, Kaituo Wang, **angyu Liu, Pontus Gourdon in P-Type ATPases (2016)

  11. No Access

    Article

    Structure and mechanism of Zn2+-transporting P-type ATPases

    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 o...

    Kaituo Wang, Oleg Sitsel, Gabriele Meloni, Henriette Elisabeth Autzen in Nature (2014)

  12. No Access

    Article

    Copper-transporting P-type ATPases use a unique ion-release pathway

    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 prev...

    Magnus Andersson, Daniel Mattle, Oleg Sitsel in Nature Structural & Molecular Biology (2014)