Publications

Cotranslational assembly of membrane protein/nanoparticles in cell-free systems

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Roman Levin, Zoe Köck, Janosch Martin, René Zangl, Theresa Gewering, Leah Schüler, Arne Moeller, Volker Dötsch, Nina Morgner, Frank Bernhard Nanoparticles composed of amphiphilic scaffold proteins and small lipid bilayers are valuable tools for reconstitution and subsequent functional and structural characterization of membrane proteins. In combination with cell-free protein production systems, nanoparticles can be used […]

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The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells

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Laura Galazzo, Gianmarco Meier, Dovile Januliene, Kristian Parey, Dario De Vecchis, Bianca Striednig, Hubert Hilbi, Lars V. Schäfer, Ilya Kuprov, Arne Moeller, Enrica Bordignon, Markus A. Seeger Membrane proteins are currently investigated after detergent extraction from native cellular membranes and reconstitution into artificial liposomes or nanodiscs, thereby removing them from their physiological environment. However, to

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Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery

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Dmitry Shvarev, Jannis Schoppe, Caroline König, Angela Perz, Nadia Füllbrunn, Stephan Kiontke, Lars Langemeyer, Dovile Januliene, Kilian Schnelle, Daniel Kümmel, Florian Fröhlich, Arne Moeller, Christian Ungermann Lysosomes are essential for cellular recycling, nutrient signaling, autophagy, and pathogenic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requires HOPS, a conserved heterohexameric tethering

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Mechanism of multimodal substrate translocation in P-glycoprotein

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Theresa Gewering, Deepali Waghray, Kristian Parey, Joel Zapata, Pengyi Zhao, Hao Chen, Dovile Januliene, Ina L. Urbatsch, Arne Moeller, Qinghai Zhang P-glycoprotein (Pgp) is a highly dynamic ATP-binding cassette transporter that confers cancer multidrug resistance and mediates the bioavailability and pharmacokinetics of many drugs. Structural and biochemical data have provided insights into the binding of

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Frozen motion: how cryo-EM changes the way we look at ABC transporters

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Dmitry Shvarev, Dovile Januliene, Arne Moeller ATP-binding cassette (ABC) transporters are widely present molecular machines that transfer substrates across the cell membrane. ABC transporters are involved in numerous physiological processes and are often clinical targets. Structural biology is fundamental to obtain the molecular details underlying ABC transporter function and suggest approaches to modulate it. Until

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Single-Particle Cryo-EM of Membrane Proteins

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Dovile Januliene and Arne Möller In the recent years, the protein databank has been fueled by the exponential growth of high-resolution electron cryo-microscopy (cryo-EM) structures. This trend will be further accelerated through the continuous software and method developments and the increasing availability of imaging centers, which will open cryo-EM to a wide array of researchers

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Cryo‐EM of ABC transporters: an ice‐cold solution to everything?

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Dovile Januliene & Arne Moeller High-resolution cryo-EM has revolutionized how we look at ABC transporters and membrane proteins in general. An ever-increasing number of software tools and faster processing now allow dissecting the molecular details of nanomachines at atomic precision. Considering the further benefits of significantly reduced sample demands and increased speed, cryo-EM will dominate

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Neue Möglichkeiten für die Strukturbestimmungvon Membranproteinen

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Theresa Gewering, Arne Möller Membrane proteins establish the connection between the outside andthe inside of a cell. Even though 30 % of proteins in a cell are membraneassociated, their structural data is strongly underrepresented due tothe high flexibility and low purification yield. The resolution revolutionin cryo-EM opened up new opportunities to solve structures of dynamicmembrane

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Structure of Merkel cell polyomavirus capsid and interaction with its 2 glycosaminoglycan attachment receptor

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Merkel cell polyomavirus (MCPyV) is a human double-stranded DNA tumor virus. MCPyV cell entry is unique among the polyomavirus family as it requires the engagement of two types of glycans, sialylated oligosaccharides and sulfated glycosaminoglycans (GAGs). Here, we present crystallographic and cryo-electron microscopic structures of the icosahedral MCPyV capsid and analysis of its glycan interactions via NMR spectroscopy.

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Structure and autoregulation of a P4-ATPase lipid flippase

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Type 4 P-type ATPases (P4-ATPases) are lipid flippases that drive the active transport of phospholipids from exoplasmic or luminal leaflets to cytosolic leaflets of eukaryotic membranes. The molecular architecture of P4-ATPases and the mechanism through which they recognize and transport lipids have remained unknown.

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