2nww: Difference between revisions

Revision as of 12:12, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nww.png

Template:STRUCTURE 2nww

Crystal structure of GltPh in complex with TBOACrystal structure of GltPh in complex with TBOA

Template:ABSTRACT PUBMED 17230192

About this StructureAbout this Structure

2NWW is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

ReferenceReference

Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter., Boudker O, Ryan RM, Yernool D, Shimamoto K, Gouaux E, Nature. 2007 Jan 25;445(7126):387-93. Epub 2007 Jan 17. PMID:17230192

Page seeded by OCA on Tue Jul 29 12:12:44 2008

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OCA

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-'''Crystal structure of GltPh in complex with TBOA'''
+===Crystal structure of GltPh in complex with TBOA===
-==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
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+{{ABSTRACT_PUBMED_17230192}}
 ==About this Structure==
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 [[Category: Inhibitor binding binding]]
 [[Category: Transmembrane transporter]]
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