2nwl

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[[Image:2nwl.gif|left|200px]]<br /><applet load="2nwl" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2nwl, resolution 2.960&Aring;" />
 
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'''Crystal structure of GltPh in complex with L-Asp'''<br />
 
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==Overview==
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==Crystal structure of GltPh in complex with L-Asp==
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<StructureSection load='2nwl' size='340' side='right'caption='[[2nwl]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2nwl]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NWL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.96&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nwl OCA], [https://pdbe.org/2nwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nwl RCSB], [https://www.ebi.ac.uk/pdbsum/2nwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nwl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLT_PYRHO GLT_PYRHO] Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake (PubMed:17435767, PubMed:19380583, PubMed:17230192, Ref.11). Has only very low glutamate transport activity (PubMed:19380583, PubMed:17230192). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting in electrogenic transport (PubMed:17435767, PubMed:19380583, Ref.11). Na(+) binding enhances the affinity for aspartate (PubMed:19380583, Ref.11). Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (PubMed:17435767). In contrast to mammalian homologs, transport does not depend on pH or K(+) ions (PubMed:19380583).<ref>PMID:17230192</ref> <ref>PMID:17435767</ref> <ref>PMID:19380583</ref> [PDB:4P19]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nw/2nwl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nwl ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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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==About this Structure==
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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<ref>PMID:17230192</ref>
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2NWL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=ASP:'>ASP</scene> and <scene name='pdbligand=PLM:'>PLM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NWL OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17230192 17230192]
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</div>
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[[Category: Pyrococcus horikoshii]]
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<div class="pdbe-citations 2nwl" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Boudker, O.]]
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[[Category: Gouaux, E.]]
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[[Category: Ryan, R.]]
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[[Category: Shimamoto, K.]]
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[[Category: Yernool, D.]]
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[[Category: ASP]]
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[[Category: PLM]]
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[[Category: alpha helical]]
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[[Category: helical hairpin]]
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[[Category: membrane protein]]
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[[Category: unwound region]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:48 2008''
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==See Also==
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*[[Symporter 3D structures|Symporter 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pyrococcus horikoshii]]
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[[Category: Boudker O]]
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[[Category: Gouaux E]]
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[[Category: Ryan R]]
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[[Category: Shimamoto K]]
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[[Category: Yernool D]]

Current revision

Crystal structure of GltPh in complex with L-Asp

PDB ID 2nwl

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