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Articles by Daniel Roderer
Atomic structure and plasticity of the CTX-MthK complex investigated by cryo-EM, NMR, and MD simulations
Abstract Scorpion toxins block potassium channels, disrupting cellular excitability and causing symptoms such as pain, muscle spasms, or paralysis. Here, we use an integrated structural biology approach to uncover the binding mode of the scorpion toxin charybdotoxin (CTX) to the MthK channel, a model system for human large-conductance potassium (BK) channels.
Spatial N-glycan rearrangement on α5β1 integrin nucleates galectin-3 oligomers to determine endocytic fate - Nature Communications
Abstract Membrane glycoproteins frequently adopt different conformations when altering between active and inactive states. Here, we discover a molecular switch that exploits dynamic spatial rearrangements of N-glycans during such conformational transitions to control protein function.
Nucleoside diphosphate kinase A (NME1) catalyses its own oligophosphorylation - Nature Chemistry
Abstract Protein phosphorylation is a central signalling mechanism in eukaryotic cells. The scope of this post-translational modification includes protein pyro- and polyphosphorylation. Here we report the discovery of another mode of phosphorylation: protein oligophosphorylation. Using site-specifically phosphorylated and pyrophosphorylated nucleoside diphosphate kinase A (NME1), the effects of these modifications on enzyme activity were investigated.
Structural basis for immune cell binding of Fusobacterium nucleatum via the trimeric autotransporter adhesin CbpF
Abstract Fusobacterium nucleatum (Fn), a commensal in the human oral cavity, is overrepresented in the colon microbiota of colorectal cancer (CRC) patients and is linked to tumor chemoresistance, metastasis, and a poor therapeutic prognosis. Fn produces numerous adhesins that mediate tumor colonization and downregulation of the host's anti-tumor immune response.
C. perfringens enterotoxin-claudin pore complex: Models for structure, mechanism of pore assembly and cation permeability
Abstract The pore-forming Clostridium perfringens enterotoxin (CPE), a common cause of foodborne diseases, facilitates Ca2+ influx in enterocytes, leading to cell damage. Upon binding to certain claudins (e.g. claudin-4), CPE forms oligomeric pores in the cell membrane. While the CPE-claudin interaction mechanism is well known, the structure and assembly of the pore complex remain elusive.
Multi-state kinetics of the syringe-like injection mechanism of Tc toxins
Abstract Tc toxins are virulence factors of many insects and human pathogenic bacteria. They attach as soluble prepores to receptors on host cells and following acidification in the late endosome, perforate the cell membrane like a syringe to translocate toxic enzymes into the host cell through their pore-forming channel.
CRISPR screens in Drosophila cells identify Vsg as a Tc toxin receptor - Nature
Abstract 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 virulence factors3,4,5,6. No protein receptors are known for any Tc toxins, which limits our understanding of their specificity and pathogenesis.
Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin - Nature Communications
Abstract Tc toxins deliver toxic enzymes into host cells by a unique injection mechanism. One of these enzymes is the actin ADP-ribosyltransferase TccC3, whose activity leads to the clustering of the cellular cytoskeleton and ultimately cell death. Here, we show in atomic detail how TccC3 modifies actin. We find that the ADP-ribosyltransferase does not bind to G-actin but interacts with two consecutive actin subunits of F-actin.
Tc toxin activation requires unfolding and refolding of a β-propeller
a, Interactions at the TcA–TcB interface. Binding of TcA to TcB–TcC is stabilized by interactions between the pseudo-six-fold symmetrical β-propeller of TcB and the five-fold symmetrical TcB-binding domain of TcA. The gatekeeper domain, shown in blue, undergoes the largest conformational changes during gate opening. In the open state, residues R485 (i) and K534 (iv) of blades 3 and 4, respectively, are positioned within negatively charged grooves of the TcB-binding domain of TcA.
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