4p6h: Difference between revisions
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''' | ==Tl+-bound inward-facing state (bound conformation) of the glutamate transporter homologue GltPh== | ||
<StructureSection load='4p6h' size='340' side='right' caption='[[4p6h]], [[Resolution|resolution]] 4.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4p6h]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P6H FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xfh|1xfh]], [[2nwl|2nwl]], [[2nww|2nww]], [[2nwx|2nwx]], [[3kbc|3kbc]], [[3v8f|3v8f]], [[3v8g|3v8g]], [[4izm|4izm]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p6h RCSB], [http://www.ebi.ac.uk/pdbsum/4p6h PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Membrane transporters that clear the neurotransmitter glutamate from synapses are driven by symport of sodium ions and counter-transport of a potassium ion. Previous crystal structures of a homologous archaeal sodium and aspartate symporter showed that a dedicated transport domain carries the substrate and ions across the membrane. Here, we report new crystal structures of this homologue in ligand-free and ions-only bound outward- and inward-facing conformations. We show that after ligand release, the apo transport domain adopts a compact and occluded conformation that can traverse the membrane, completing the transport cycle. Sodium binding primes the transport domain to accept its substrate and triggers extracellular gate opening, which prevents inward domain translocation until substrate binding takes place. Furthermore, we describe a new cation-binding site ideally suited to bind a counter-transported ion. We suggest that potassium binding at this site stabilizes the translocation-competent conformation of the unloaded transport domain in mammalian homologues. | |||
Coupled ion binding and structural transitions along the transport cycle of glutamate transporters.,Verdon G, Oh S, Serio RN, Boudker O Elife. 2014 May 19:e02283. doi: 10.7554/eLife.02283. PMID:24842876<ref>PMID:24842876</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Boudker, O]] | |||
[[Category: Verdon, G]] | |||
[[Category: Transport protein]] | |||
Revision as of 08:07, 4 June 2014
Tl+-bound inward-facing state (bound conformation) of the glutamate transporter homologue GltPhTl+-bound inward-facing state (bound conformation) of the glutamate transporter homologue GltPh
Structural highlights
Publication Abstract from PubMedMembrane transporters that clear the neurotransmitter glutamate from synapses are driven by symport of sodium ions and counter-transport of a potassium ion. Previous crystal structures of a homologous archaeal sodium and aspartate symporter showed that a dedicated transport domain carries the substrate and ions across the membrane. Here, we report new crystal structures of this homologue in ligand-free and ions-only bound outward- and inward-facing conformations. We show that after ligand release, the apo transport domain adopts a compact and occluded conformation that can traverse the membrane, completing the transport cycle. Sodium binding primes the transport domain to accept its substrate and triggers extracellular gate opening, which prevents inward domain translocation until substrate binding takes place. Furthermore, we describe a new cation-binding site ideally suited to bind a counter-transported ion. We suggest that potassium binding at this site stabilizes the translocation-competent conformation of the unloaded transport domain in mammalian homologues. Coupled ion binding and structural transitions along the transport cycle of glutamate transporters.,Verdon G, Oh S, Serio RN, Boudker O Elife. 2014 May 19:e02283. doi: 10.7554/eLife.02283. PMID:24842876[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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