News

The structure of the Orm2-containing serine palmitoyltransferase complex reveals distinct inhibitory potentials of yeast Orm proteins.

Carolin Körner, Jan-Hannes Schäfer, Bianca M. Escha , Kristian Parey, Stefan Walter, David Teis, Dovile Januliene, Oliver Schmidte, Arne Moellerb, Florian Fröhlich The levels of sphingolipids are crucial determinants of neurodegenerative disorders. Therefore, sphingolipid levels have to be tightly regulated. The Orm protein family and ceramides act as inhibitors in the rate-limiting step of sphingolipid […]

The structure of the Orm2-containing serine palmitoyltransferase complex reveals distinct inhibitory potentials of yeast Orm proteins. Read More »

Structural basis of the allosteric regulation of cyanobacterial glucose-6-phosphate dehydrogenase by the redox sensor OpcA

Sofia Doello, Dmitry Shvarev, Marius Theune , Jakob Sauerwein, Alexander Klon, Erva Keskin, Marko Boehm, Kirstin Gutekunst, and Karl Forchhammera The oxidative pentose phosphate (OPP) pathway is a fundamental carbon catabolic route for generating reducing power and metabolic intermediates for biosynthetic processes. In addition, its first two reactions form the OPP shunt, which replenishes the

Structural basis of the allosteric regulation of cyanobacterial glucose-6-phosphate dehydrogenase by the redox sensor OpcA Read More »

Cryo-EM structure of cell-free synthesized human histamine H2 receptor coupled to heterotrimeric Gs protein in lipid nanodisc environment

Zoe Köck, Kilian Schnelle, Margherita Persechino, Simon Umbach, Hannes Schihada, Dovile Januliene, Kristian Parey, Steffen Pockes, Peter Kolb, Volker Dötsch, ArneMöller, Daniel Hilger, Frank Bernhard Here we describe the cryo-electron microscopy structure of the human histamine 2 receptor (H2R) in an active conformation with bound histamine and in complex with Gs heterotrimeric protein at an overall

Cryo-EM structure of cell-free synthesized human histamine H2 receptor coupled to heterotrimeric Gs protein in lipid nanodisc environment Read More »

Structure of the yeast ceramide synthase

Jan-Hannes Schäfer Lena Clausmeyer, Carolin Körner, Bianca M. Esch , Verena N. Wolf , Stefan Walter, Dovile Januliene, Arne Moeller, Florian Fröhlich Ceramides play a pivotal role as essential lipids, serving as foundational components for complex sphingolipids and potent signaling molecules. Ceramides are the products of the N-acylation of a sphingoid base and a CoA-activated

Structure of the yeast ceramide synthase Read More »

Structure of the endosomal CORVET tethering complex

Dmitry Shvarev, Caroline König, Nicole Susan, Lars Langemeyer, Stefan Walter, Angela Perz, Florian Fröhlich, Christian Ungermann, Arne Moeller Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion steps. Early endosome fusion is promoted by the Rab5 GTPase and

Structure of the endosomal CORVET tethering complex Read More »

Structure of the ceramide-bound SPOTS complex

Jan-Hannes Schäfer, Carolin Körner, Bianca M. Esch, Sergej Limar, KristianParey, Stefan Walter, Dovile Januliene#, Arne Moeller#, Florian Fröhlich# Sphingolipids are structural membrane components that also function in cellular stress responses. The serine palmitoyl-transferase (SPT) catalyzes the rate limiting step in sphingolipid biogenesis. Its activity is tightly regulated through multiple binding partners, including Tsc3, Orm proteins,

Structure of the ceramide-bound SPOTS complex Read More »

Conformational variability of cyanobacterial ChlI, the AAA+ motor of magnesium chelatase involved in chlorophyll biosynthesis

Dmitry Shvarev, Alischa Ira Scholz, Arne Moeller Magnesium chelatase is a conserved enzyme complex responsible for the first committed step of chlorophyll biosynthesis in photosynthetic organisms, which is the addition of magnesium to the chlorophyll precursor, protoporphyrin IX. The complex is composed of the catalytic subunit ChlH, the bridging subunit ChlD, and the subunit ChlI,

Conformational variability of cyanobacterial ChlI, the AAA+ motor of magnesium chelatase involved in chlorophyll biosynthesis Read More »

Yck3 casein kinase-mediated phosphorylation determines Ivy1 localization and function at endosomes and vacuole

Sophie Grziwa, Jan-Hannes Schäfer, Raffaele Nicastro, Annabel Arens, Claudio De Virgilio, Florian Fröhlich, Arne Moeller, Jieqiong Gao, Lars Langemeyer, Christian Ungermann The casein kinase Yck3 is a central regulator at the vacuole that phosphorylates several proteins involved in membrane trafficking. Here, we set out to identify novel substrates. We localized endogenously tagged Yck3 not only

Yck3 casein kinase-mediated phosphorylation determines Ivy1 localization and function at endosomes and vacuole Read More »

Structure of the metazoan Rab7 GEF complex Mon1–Ccz1–Bulli

Eric Herrmann, Jan-Hannes Schäfer, Stephan Wilmes, Christian Ungermann, Arne Moeller, and Daniel Kümmel The endosomal system of eukaryotic cells represents a central sorting and recycling compartment linked to metabolic signaling and the regulation of cell growth. Tightly controlled activation of Rab GTPases is required to establish the different domains of endosomes and lysosomes. In metazoans,

Structure of the metazoan Rab7 GEF complex Mon1–Ccz1–Bulli Read More »

Regulatory sites in the Mon1-Ccz1 complex control Rab5 to Rab7 transition and endosome maturation

Ann-Christin Borchers, Maren Janz, Jan-Hannes Schäfer, Arne Moeller, Daniel Kümmel, Achim Paululat, Christian Ungermann, Lars Langemeyer Maturation from early to late endosomes depends on the exchange of their marker proteins Rab5 to Rab7. This requires Rab7 activation by its specific guanine nucleotide exchange factor (GEF) Mon1- Ccz1. Efficient GEF activity of this complex on membranes

Regulatory sites in the Mon1-Ccz1 complex control Rab5 to Rab7 transition and endosome maturation Read More »