Arne Möller

Single-Particle Cryo-EM of Membrane Proteins

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?

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

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

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.

Conformation space of a heterodimeric ABC exporter under turnover conditions.

Our findings reveal that phosphate release, not ATP hydrolysis, triggers the return of the exporter to the IF conformation. By mapping the conformational landscape during active turnover, aided by mutational and chemical modulation of kinetic rates to trap the key intermediates, we resolved fundamental steps of the substrate translocation cycle of asymmetric ABC transporters.