Transport mechanism of a bacterial homologue of glutamate transporters

Nicolas Reyes, Christopher Ginter and Olga Boudker ()
Additional contact information
Nicolas Reyes: Weill Cornell Medical College, 1300 York Avenue, Box 75, New York, New York 10065, USA
Christopher Ginter: Weill Cornell Medical College, 1300 York Avenue, Box 75, New York, New York 10065, USA
Olga Boudker: Weill Cornell Medical College, 1300 York Avenue, Box 75, New York, New York 10065, USA

Nature, 2009, vol. 462, issue 7275, 880-885

Abstract: Abstract Glutamate transporters are integral membrane proteins that catalyse a thermodynamically uphill uptake of the neurotransmitter glutamate from the synaptic cleft into the cytoplasm of glia and neuronal cells by harnessing the energy of pre-existing electrochemical gradients of ions. Crucial to the reaction is the conformational transition of the transporters between outward and inward facing states, in which the substrate binding sites are accessible from the extracellular space and the cytoplasm, respectively. Here we describe the crystal structure of a double cysteine mutant of a glutamate transporter homologue from Pyrococcus horikoshii, GltPh, which is trapped in the inward facing state by cysteine crosslinking. Together with the previously determined crystal structures of GltPh in the outward facing state, the structure of the crosslinked mutant allows us to propose a molecular mechanism by which GltPh and, by analogy, mammalian glutamate transporters mediate sodium-coupled substrate uptake.

Date: 2009
References: Add references at CitEc
Citations: View citations in EconPapers (7)

Downloads: (external link)
https://www.nature.com/articles/nature08616 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:462:y:2009:i:7275:d:10.1038_nature08616

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature08616

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().