2nwl
From Proteopedia
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|PDB= 2nwl |SIZE=350|CAPTION= <scene name='initialview01'>2nwl</scene>, resolution 2.960Å | |PDB= 2nwl |SIZE=350|CAPTION= <scene name='initialview01'>2nwl</scene>, resolution 2.960Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene> | + | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1xfh|1xfh]], [[2nww|2NWW]], [[2nwx|2NWX]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nwl OCA], [http://www.ebi.ac.uk/pdbsum/2nwl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nwl RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Shimamoto, K.]] | [[Category: Shimamoto, K.]] | ||
[[Category: Yernool, D.]] | [[Category: Yernool, D.]] | ||
| - | [[Category: ASP]] | ||
| - | [[Category: PLM]] | ||
[[Category: alpha helical]] | [[Category: alpha helical]] | ||
[[Category: helical hairpin]] | [[Category: helical hairpin]] | ||
| Line 34: | Line 35: | ||
[[Category: unwound region]] | [[Category: unwound region]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:09:24 2008'' |
Revision as of 01:09, 31 March 2008
| |||||||
| , resolution 2.960Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1xfh, 2NWW, 2NWX
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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