2nwl: Difference between revisions

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[[Image:2nwl.gif|left|200px]]
{{Seed}}
[[Image:2nwl.png|left|200px]]


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{{STRUCTURE_2nwl|  PDB=2nwl  |  SCENE=  }}  
{{STRUCTURE_2nwl|  PDB=2nwl  |  SCENE=  }}  


'''Crystal structure of GltPh in complex with L-Asp'''
===Crystal structure of GltPh in complex with L-Asp===




==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.
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{{ABSTRACT_PUBMED_17230192}}


==About this Structure==
==About this Structure==
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[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: Unwound region]]
[[Category: Unwound region]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:00:05 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:20:07 2008''

Revision as of 12:20, 29 July 2008

File:2nwl.png

Template:STRUCTURE 2nwl

Crystal structure of GltPh in complex with L-Asp

Template:ABSTRACT PUBMED 17230192

About this Structure

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

Reference

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

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