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1xfh

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[[Image:1xfh.png|left|200px]]
 
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{{STRUCTURE_1xfh| PDB=1xfh | SCENE= }}
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==Structure of glutamate transporter homolog from Pyrococcus horikoshii==
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<StructureSection load='1xfh' size='340' side='right'caption='[[1xfh]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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===Structure of glutamate transporter homolog from Pyrococcus horikoshii===
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xfh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XFH FirstGlance]. <br>
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{{ABSTRACT_PUBMED_15483603}}
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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]] 3.5&#8491;</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=1xfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfh OCA], [https://pdbe.org/1xfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xfh RCSB], [https://www.ebi.ac.uk/pdbsum/1xfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfh ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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[[1xfh]] is a 3 chain structure with 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=1XFH OCA].
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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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==Reference==
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== Evolutionary Conservation ==
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<ref group="xtra">PMID:015483603</ref><references group="xtra"/>
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Pyrococcus horikoshii]]
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Check<jmol>
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[[Category: Boudker, O.]]
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<jmolCheckbox>
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[[Category: Gouaux, E.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/1xfh_consurf.spt"</scriptWhenChecked>
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[[Category: Jin, Y.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Yernool, D.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: Transport protein]]
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</jmolCheckbox>
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[[Category: Trimeric helical transmembrane protein]]
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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=1xfh ConSurf].
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<div style="clear:both"></div>
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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 OT3]]
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[[Category: Boudker O]]
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[[Category: Gouaux E]]
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[[Category: Jin Y]]
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[[Category: Yernool D]]

Current revision

Structure of glutamate transporter homolog from Pyrococcus horikoshii

PDB ID 1xfh

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