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| [[Image:2nwx.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2nwx| PDB=2nwx | SCENE= }} | | {{STRUCTURE_2nwx| PDB=2nwx | SCENE= }} |
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| '''Crystal structure of GltPh in complex with L-aspartate and sodium ions'''
| | ===Crystal structure of GltPh in complex with L-aspartate and sodium ions=== |
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| ==Overview==
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| Secondary transporters are integral membrane proteins that catalyse the movement of substrate molecules across the lipid bilayer by coupling substrate transport to one or more ion gradients, thereby providing a mechanism for the concentrative uptake of substrates. Here we describe crystallographic and thermodynamic studies of Glt(Ph), a sodium (Na+)-coupled aspartate transporter, defining sites for aspartate, two sodium ions and d,l-threo-beta-benzyloxyaspartate, an inhibitor. We further show that helical hairpin 2 is the extracellular gate that controls access of substrate and ions to the internal binding sites. At least two sodium ions bind in close proximity to the substrate and these sodium-binding sites, together with the sodium-binding sites in another sodium-coupled transporter, LeuT, define an unwound alpha-helix as the central element of the ion-binding motif, a motif well suited to the binding of sodium and to participation in conformational changes that accompany ion binding and unbinding during the transport cycle.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17230192}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17230192 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17230192}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Substrate binding]] | | [[Category: Substrate binding]] |
| [[Category: Transmembrane transporter]] | | [[Category: Transmembrane transporter]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:00:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:42:23 2008'' |