TL;DR
Findings provide direct experimental evidence that the α-1 helix participates in ABC transporter-mediated membrane insertion and pore formation through its translocation, thereby advancing the understanding of the molecular mechanism underlying Cry toxin pore assembly.
Comparative structural analysis revealed that the prepore-to-pore transition proceeds through stepwise, domino-like conformational changes, providing a framework for understanding PFP maturation and for engineering membrane pores with controlled assembly, stability and lumen architecture properties.
Using a live-cell lipid reporter, membrane order probe, and surface proteome mapping, it is shown that TMEM30A-knockout cells display robust PS externalization accompanied by faster lateral diffusion of membrane constituents and decreased plasma membrane order.
Results suggest that the interaction of Cry4Aa with N-acetylgalactosamine moieties is a vital step in the process of pore formation, and may induce a conformational change in the Cry4Aa molecule that facilitates its insertion into the target membrane.
ABSTRACT SARS-CoV-2 entry into host cells is mediated by the spike glycoprotein, which promotes fusion between viral and host membranes. Despite its importance, the precise location and mode of action of the fusion peptide, a key spike region that inserts into and perturbs the host membrane, remain elusive. Two regions...
The integrative structural model of full-length HsNHE6 provides a framework for understanding HsNHE6-mediated ion exchange and its disruption in Christianson syndrome and shows a kinetic preference for K+ over Na+ transport.
The findings extend the mechanistic understanding of Rab7 beyond its catalytic pocket and establish the AflRab7 C-terminal IDR as a critical regulatory element that couples vacuolar dynamics to A. flavus development and aflatoxin biosynthesis, highlighting a tractable target for mitigating fungal toxigenic potential.
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