Date

January 2011

Document Type

Dissertation

Degree Name

Ph.D.

Department

Dept. of Biochemistry and Molecular Biology

Institution

Oregon Health & Science University

Abstract

The mechanism of ion-coupled secondary transport is universally utilized in every kingdom of life to catalyze the concentrative uptake of molecules across cellular membranes. Ion-coupled transporters are central to many physiological functions ranging from nutrient uptake to neural synaptic transmission. Recently, the crystal structure of the ion-coupled transporter LeuT, a bacterial homolog of the Neurotransmitter:Sodium Symporter (NSS) family, was solved. This structure revealed a novel transporter motif characterized by an internal 2-fold structural repeat, with the substrate L-leucine and two sodium ions bound in a centrally located occluded binding site, suggestive of an alternating access transport mechanism. To date, LeuT presents one of only a small handful of sodium-coupled secondary transporters structures, and remains the only NSS transporter to have yielded to crystallographic studies. LeuT has therefore become widely used as the structural blueprint for modeling and interp

Identifier

doi:10.6083/M4XS5SDX

School

School of Medicine

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