2nwl
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2nwl.gif|left|200px]] | + | [[Image:2nwl.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of GltPh in complex with L-Asp''' | + | {{Structure |
| + | |PDB= 2nwl |SIZE=350|CAPTION= <scene name='initialview01'>2nwl</scene>, resolution 2.960Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene> and <scene name='pdbligand=PLM:PALMITIC ACID'>PLM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of GltPh in complex with L-Asp''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2NWL is a [ | + | 2NWL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NWL OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17230192 17230192] |
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: unwound region]] | [[Category: unwound region]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:52:05 2008'' |
Revision as of 15:52, 20 March 2008
| |||||||
| , resolution 2.960Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of GltPh in complex with L-Asp
Overview
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.
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
Page seeded by OCA on Thu Mar 20 17:52:05 2008
