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Substrate releasing or inhibitor binding on the intracellular side of a glutamate transporter homologue require movements of the transport domain through the lipid membrane, which undergoes adaptive deformations.

The cryo-EM structure and functional characterization of the chloride-selective ion transporter Slc26a9 defines its oligomeric architecture and transport mechanism.

A magnesium transporter from Escherichia coli depends strongly on the lipid cardiolipin and acts both as a sensor and a transporter of magnesium.

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.

A detailed molecular mechanism on lipid flipping from outside leaflet to the inside leaflet of the eukaryotic plasma membrane bilayer.

Sterol transport by Niemann-Pick type C proteins induces the expansion of raft-like domains in the yeast vacuole, enabling engulfment of lipid droplets by microautophagy.

The structure of an NRAMP-related Al³⁺ transporter illustrates the evolution of a branch of a conserved protein family of metal ion transporters in plants to combat Al³⁺ toxicity in acidic soil.

The structure of the potassium-chloride cotransporter KCC4 provides insight into the basis of ion specificity, transport stoichiometry, and activity regulation for a broadly physiologically and clinically important transporter family.

The amino acids that are necessary for phospholipid scrambling by ANO6/TMEM16F can, via domain swapping, confer scrambling activity to the chloride ion channel ANO1 that normally does not scramble phospholipids.

Structure of the dimeric Haemophilus influenzae TRAP transporter (SiaQM) reveals two Na⁺ sites, the substrate-binding site and lipid-binding sites, and weak but promiscuous binding of SiaP to SiaQM.