David Wöhlert, Maria J Grötzinger ... Özkan Yildiz
The high-resolution x-ray structure of an asymmetrical SeCitS dimer, present in the inward- and outward-facing state, provides a complete mechanism of substrate and ion translocation in a sodium-dependent symporter.
Computational approach shows that the occluded state in GLUT transporters is equivalent to the transition state of soluble enzymes and this has the highest affinity for the substrate sugar.
Marco van den Noort, Panagiotis Drougkas ... Bert Poolman
Transient and weak interactions between the substrate-binding proteins of the ATP-binding cassette transporter OpuA can influence the transport efficiency.
Salvatore Assenza, Alberto Stefano Sassi ... Alessandro Barducci
A multiscale modeling approach reveals how the energy from ATP hydrolysis is used by Hsp70 chaperones to remodel the conformation of their substrates through a novel force-generating mechanism.
An unexpected new biological function was discovered for the universally conserved cofactor lipoate, as lipoate-binding proteins proved essential for a novel wide-spread prokaryotic sulfur oxidation pathway.
Sodium ions control the rates of both substrate binding and dissociation of an archaeal homologue of glutamate transporters in a manner that minimizes binding intermediates and maximizes transport efficiency.
C-terminal phosphorylation of the lipid phosphatase PTEN drives a reduction in membrane affinity and leads to a more compact conformation that involves a C2 domain-tail interaction.
The chaperone protein BiP forms complexes with Ire1 and Perk that dissociate when unfolded proteins bind to BiP to activate the unfolded protein response in the ER.
