Titre
Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1.
Type
article
Institution
Externe
Auteur(s)
Margittai, M.
Auteure/Auteur
Widengren, J.
Auteure/Auteur
Schweinberger, E.
Auteure/Auteur
Schröder, G.F.
Auteure/Auteur
Felekyan, S.
Auteure/Auteur
Haustein, E.
Auteure/Auteur
König, M.
Auteure/Auteur
Fasshauer, D.
Auteure/Auteur
Grubmüller, H.
Auteure/Auteur
Jahn, R.
Auteure/Auteur
Seidel, C.A.
Auteure/Auteur
Liens vers les personnes
ISSN
0027-8424
Statut éditorial
Publié
Date de publication
2003
Volume
100
Numéro
26
Première page
15516
Dernière page/numéro d’article
15521
Peer-reviewed
Oui
Langue
anglais
Résumé
Protein conformational transitions form the molecular basis of many cellular processes, such as signal transduction and membrane traffic. However, in many cases, little is known about their structural dynamics. Here we have used dynamic single-molecule fluorescence to study at high time resolution, conformational transitions of syntaxin 1, a soluble N-ethylmaleimide-sensitive factor attachment protein receptors protein essential for exocytotic membrane fusion. Sets of syntaxin double mutants were randomly labeled with a mix of donor and acceptor dye and their fluorescence resonance energy transfer was measured. For each set, all fluorescence information was recorded simultaneously with high time resolution, providing detailed information on distances and dynamics that were used to create structural models. We found that free syntaxin switches between an inactive closed and an active open configuration with a relaxation time of 0.8 ms, explaining why regulatory proteins are needed to arrest the protein in one conformational state.
PID Serval
serval:BIB_8C255D6C2AD6
PMID
Open Access
Oui
Date de création
2011-09-15T08:16:06.165Z
Date de création dans IRIS
2025-05-20T22:35:15Z