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6wyk
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the GltPh L152C-G321C mutant in the intermediate chloride conducting state.== | |
| + | <StructureSection load='6wyk' size='340' side='right'caption='[[6wyk]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6wyk]] is a 1 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=6WYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WYK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene></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=6wyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wyk OCA], [https://pdbe.org/6wyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wyk RCSB], [https://www.ebi.ac.uk/pdbsum/6wyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wyk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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] | ||
| - | + | ==See Also== | |
| - | + | *[[Symporter 3D structures|Symporter 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Chen | + | </StructureSection> |
| - | [[Category: Font | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Pyrococcus horikoshii OT3]] |
| - | [[Category: | + | [[Category: Chen I]] |
| + | [[Category: Font J]] | ||
| + | [[Category: Ryan RM]] | ||
| + | [[Category: Sobti M]] | ||
| + | [[Category: Stewart AG]] | ||
Current revision
Cryo-EM structure of the GltPh L152C-G321C mutant in the intermediate chloride conducting state.
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