Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter: Sodium symporter

Christian B. Billesbølle, Mie B. Krüger, Lei Shi, Matthias Quick, Zheng Li, Sebastian Stolzenberg, Julie Kniazeff, Kamil Gotfryd, Jonas S. Mortensen, Jonathan A. Javitch, Harel Weinstein, Claus J. Loland, Ulrik Gether

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Background: The mechanism coupling substrate binding to transport in neurotransmitter: sodium symporters (NSSs) is poorly understood. Results: Site-directed fluorescence quenching spectroscopy experiments on the NSS homologue LeuT reveal a structural intermediate preceding transition to the inward-open conformation. Conclusion: Stability of the intermediate might represent a rate-limiting barrier in the transport mechanism. Significance: The data add to our mechanistic understanding of Na+-coupled transport across lipid bilayers.

Original languageEnglish (US)
Pages (from-to)26725-26738
Number of pages14
JournalJournal of Biological Chemistry
Volume290
Issue number44
DOIs
StatePublished - Oct 30 2015

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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