O
Olga Boudker
Researcher at Cornell University
Publications - 41
Citations - 3665
Olga Boudker is an academic researcher from Cornell University. The author has contributed to research in topics: Symporter & Integral membrane protein. The author has an hindex of 20, co-authored 37 publications receiving 3208 citations. Previous affiliations of Olga Boudker include Howard Hughes Medical Institute & Johns Hopkins University.
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Structure of a glutamate transporter homologue from Pyrococcus horikoshii
TL;DR: This work presents the crystal structure of a eukaryotic glutamate transporter homologue from Pyrococcus horikoshii and proposes that transport of glutamate is achieved by movements of the hairpins that allow alternating access to either side of the membrane.
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Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
Olga Boudker,Renae M. Ryan,Renae M. Ryan,Dinesh Yernool,Dinesh Yernool,Keiko Shimamoto,Eric Gouaux,Eric Gouaux,Eric Gouaux +8 more
TL;DR: In this article, the authors describe crystallographic and thermodynamic studies of Glt(Ph), a sodium (Na+)-coupled aspartate transporter, defining sites for aspartates, two sodium ions and d,l-threo-beta-benzyloxyaspartate, an inhibitor.
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Transport mechanism of a bacterial homologue of glutamate transporters
TL;DR: The crystal structure of a double cysteine mutant of a glutamate transporter homologue from Pyrococcus horikoshii is described, which allows for a molecular mechanism by which GltPh and, by analogy, mammalian glutamate transporters mediate sodium-coupled substrate uptake.
Journal ArticleDOI
Shared Molecular Mechanisms of Membrane Transporters
David A. Drew,Olga Boudker +1 more
TL;DR: This review compares and contrast rocker-switch, rocking-bundle, and elevator alternating-access mechanisms to highlight shared features and novel refinements to the basic alternating- access model.
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Transport dynamics in a glutamate transporter homologue
TL;DR: It is proposed that the switch to the dynamic mode in glutamate transporters is due to separation of the transport domain from the trimeric scaffold, which precedes domain movements across the bilayer, which is approximately 100-fold slower than subsequent transmembrane movements.