2a65
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2a65.gif|left|200px]] | [[Image:2a65.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2a65", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2a65| PDB=2a65 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of LEUTAA, a bacterial homolog of Na+/Cl--dependent neurotransmitter transporters''' | '''Crystal structure of LEUTAA, a bacterial homolog of Na+/Cl--dependent neurotransmitter transporters''' | ||
| Line 30: | Line 27: | ||
[[Category: Singh, S K.]] | [[Category: Singh, S K.]] | ||
[[Category: Yamashita, A.]] | [[Category: Yamashita, A.]] | ||
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:39:20 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:39, 3 May 2008
Crystal structure of LEUTAA, a bacterial homolog of Na+/Cl--dependent neurotransmitter transporters
Overview
Na+/Cl--dependent transporters terminate synaptic transmission by using electrochemical gradients to drive the uptake of neurotransmitters, including the biogenic amines, from the synapse to the cytoplasm of neurons and glia. These transporters are the targets of therapeutic and illicit compounds, and their dysfunction has been implicated in multiple diseases of the nervous system. Here we present the crystal structure of a bacterial homologue of these transporters from Aquifex aeolicus, in complex with its substrate, leucine, and two sodium ions. The protein core consists of the first ten of twelve transmembrane segments, with segments 1-5 related to 6-10 by a pseudo-two-fold axis in the membrane plane. Leucine and the sodium ions are bound within the protein core, halfway across the membrane bilayer, in an occluded site devoid of water. The leucine and ion binding sites are defined by partially unwound transmembrane helices, with main-chain atoms and helix dipoles having key roles in substrate and ion binding. The structure reveals the architecture of this important class of transporter, illuminates the determinants of substrate binding and ion selectivity, and defines the external and internal gates.
About this Structure
2A65 is a Single protein structure of sequence from Aquifex aeolicus vf5. Full crystallographic information is available from OCA.
Reference
Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters., Yamashita A, Singh SK, Kawate T, Jin Y, Gouaux E, Nature. 2005 Sep 8;437(7056):215-23. Epub 2005 Jul 24. PMID:16041361 Page seeded by OCA on Sat May 3 18:39:20 2008
