1xfh: Difference between revisions

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[[Image:1xfh.png|left|200px]]


{{STRUCTURE_1xfh|  PDB=1xfh  |  SCENE=  }}
==Structure of glutamate transporter homolog from Pyrococcus horikoshii==
 
<StructureSection load='1xfh' size='340' side='right'caption='[[1xfh]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
===Structure of glutamate transporter homolog from Pyrococcus horikoshii===
== Structural highlights ==
 
<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>
{{ABSTRACT_PUBMED_15483603}}
</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>
 
<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>
==About this Structure==
</table>
[[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].  
== Function ==
 
[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]
==Reference==
== Evolutionary Conservation ==
<ref group="xtra">PMID:015483603</ref><references group="xtra"/>
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Pyrococcus horikoshii]]
Check<jmol>
[[Category: Boudker, O.]]
  <jmolCheckbox>
[[Category: Gouaux, E.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/1xfh_consurf.spt"</scriptWhenChecked>
[[Category: Jin, Y.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Yernool, D.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Transport protein]]
  </jmolCheckbox>
[[Category: Trimeric helical transmembrane protein]]
</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].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Boudker O]]
[[Category: Gouaux E]]
[[Category: Jin Y]]
[[Category: Yernool D]]

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