O. Boudker

Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters

The paper uses phylogenetics and ancestral protein reconstruction to show that sodium-dependent substrate binding in glutamate transporters evolved before changes in coupling mechanisms.

Dancing with the ions: symport and antiport mechanisms of human glutamate transporters

This study presents high-resolution Cryo-EM structures of human EAAT3 to elucidate the symport and antiport mechanisms of glutamate transporters.

An environmentally ultrasensitive fluorine probe to resolve protein conformational ensembles by 19F NMR and cryo-EM

This paper introduces a fluorine probe that enhances 19F NMR sensitivity for studying protein conformational changes, validated by cryo-EM structural analysis.

Heterogeneous substrate binding in a glutamate transporter homologue

The paper investigates substrate binding heterogeneity in the glutamate transporter homologue GltPh, revealing sub-states with different affinities and structural changes upon substrate binding.

Transport mechanism of the neuronal excitatory amino acid transporter

The paper reports Cryo-EM structures of hEAAT3 in different functional states, revealing an elevator mechanism for glutamate transport and conserved sodium-substrate coupling.

Large domain movements through lipid bilayer mediate substrate release and inhibition of glutamate transporters

This study reports Cryo-EM structures of GltPh to elucidate domain movements and their role in substrate release and inhibition.

The high-energy transition state of a membrane transporter

The paper identifies the high-energy transition state of a membrane transporter and proposes an approach for allosteric modulation based on structural analysis.

Monitoring Dynamics of Large Membrane Proteins by 19F Paramagnetic Longitudinal Relaxation: Domain Movement in a Glutamate Transporter Homolog

The paper uses 19F-NMR and Cryo-EM to study conformational dynamics of a glutamate transporter homolog, identifying three states and measuring conformational exchange rates.