Editor's Summary
8 September 2005
Neurotransmission
The crystal structure of a bacterial protein related to sodium- and chloride-dependent neurotransmitter transporters has been determined. In the brain these transporters use electrochemical gradients to drive rapid uptake of neurotransmitters such as serotonin, dopamine, 
-amino butyric acid and glycine at synapses, bringing neurotransmission to an end. The bacterial homologue, from the hyperthermophile Aquifex aeolicus, transports leucine (in the centre of the ribbon structure on the cover) across the cell membrane. Its structure reveals the binding sites for the Na+ ions and leucine, together with the 'gates' that open to allow access to these sites. Knowledge of this structure is important for many aspects of drug design: these transporters are targets for antidepressants and drugs of abuse and their dysfunction is involved in neurological disorders including Parkinson's disease and epilepsy.
News and Views: Molecular physiology: Intimate contact enables transport
Sodium-coupled neurotransmitter transporters are essential for neurons to communicate. The high-resolution crystal structure of a bacterial relative hints at how this family of transporters works.
Baruch I. Kanner
doi: 10.1038/437203a
Article: Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters
Atsuko Yamashita, Satinder K. Singh, Toshimitsu Kawate, Yan Jin and Eric Gouaux
doi: 10.1038/nature03978
Abstract | Full Text | PDF (1,027K) | Supplementary information