Conformational heterogeneity of the aspartate transporter Glt(Ph)

Inga Hänelt, Dorith Wunnicke, Enrica Bordignon, Heinz-Juergen Steinhoff, Dirk Jan Slotboom*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

93 Citaten (Scopus)
624 Downloads (Pure)


Glt(Ph) is a Pyrococcus horikoshii homotrimeric Na+-coupled aspartate transporter that belongs to the glutamate transporter family. Each protomer consists of a trimerization domain involved in subunit interaction and a transporting domain with the substrate-binding site. Here, we have studied the conformational changes underlying transport by Gltph using [PR spectroscopy. The trimerization domains form a rigid scaffold, whereas the transporting domains sample multiple conformations, consistent with large-scale movements during the transport cycle. Binding of substrates changed the occupancies of the different conformational states, but the domains remained heterogeneous. The membrane environment favored conformations different from those observed in detergent micelles, but the transporting domain remained structurally heterogeneous in both environments. We conclude that the transporting domains sample multiple conformational states with substantial occupancy regardless of the presence of substrate and coupling ions, consistent with equilibrium constants close to unity between the observed transporter conformations.

Originele taal-2English
Pagina's (van-tot)210-214
Aantal pagina's5
TijdschriftNature Structural & Molecular Biology
Nummer van het tijdschrift2
StatusPublished - feb.-2013

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