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


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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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== 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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</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>
{{STRUCTURE_1xfh|  PDB=1xfh  |  SCENE=  }}
</table>
 
== Function ==
===Structure of glutamate transporter homolog from Pyrococcus horikoshii===
[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]
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
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==About this Structure==
</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].
1XFH is a [[Single protein]] structure of sequence from [http://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].  
<div style="clear:both"></div>
 
== References ==
==Reference==
<references/>
Structure of a glutamate transporter homologue from Pyrococcus horikoshii., Yernool D, Boudker O, Jin Y, Gouaux E, Nature. 2004 Oct 14;431(7010):811-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15483603 15483603]
__TOC__
[[Category: Pyrococcus horikoshii ot3]]
</StructureSection>
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Boudker, O.]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Gouaux, E.]]
[[Category: Boudker O]]
[[Category: Jin, Y.]]
[[Category: Gouaux E]]
[[Category: Yernool, D.]]
[[Category: Jin Y]]
[[Category: Trimeric helical transmembrane protein]]
[[Category: Yernool D]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:57:02 2008''

Latest revision as of 11:50, 14 February 2024

Structure of glutamate transporter homolog from Pyrococcus horikoshiiStructure of glutamate transporter homolog from Pyrococcus horikoshii

Structural highlights

1xfh is a 3 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3] [PDB:4P19]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Boudker O, Ryan RM, Yernool D, Shimamoto K, Gouaux E. Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature. 2007 Jan 25;445(7126):387-93. Epub 2007 Jan 17. PMID:17230192 doi:10.1038/nature05455
  2. ↑ Ryan RM, Mindell JA. The uncoupled chloride conductance of a bacterial glutamate transporter homolog. Nat Struct Mol Biol. 2007 May;14(5):365-71. doi: 10.1038/nsmb1230. Epub 2007 Apr , 15. PMID:17435767 doi:http://dx.doi.org/10.1038/nsmb1230
  3. ↑ Ryan RM, Compton EL, Mindell JA. Functional characterization of a Na+-dependent aspartate transporter from Pyrococcus horikoshii. J Biol Chem. 2009 Jun 26;284(26):17540-8. doi: 10.1074/jbc.M109.005926. Epub 2009, Apr 20. PMID:19380583 doi:http://dx.doi.org/10.1074/jbc.M109.005926

1xfh, resolution 3.50Å

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