6ctf: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6ctf is ~~ON HOLD until Paper Publication~~

==Crystal structure of GltPh fast mutant - R276S/M395R==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[6ctf]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CTF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CTF FirstGlance]. <br>

~~Description~~:

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ctf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ctf OCA], [http://pdbe.org/6ctf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ctf RCSB], [http://www.ebi.ac.uk/pdbsum/6ctf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ctf ProSAT]</span></td></tr>

</table>

== Function ==

[[http://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]

== References ==

__TOC__

</StructureSection>

[[Category: Boudker, O]]

[[Category: Oh, S]]

[[Category: Ligand-bound]]

[[Category: Membrane protein]]

[[Category: Transporter]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6ctf is ON HOLD  until Paper Publication
+==Crystal structure of GltPh fast mutant - R276S/M395R==
+<StructureSection load='6ctf' size='340' side='right' caption='[[6ctf]], [[Resolution|resolution]] 4.05&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ctf]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CTF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CTF FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ctf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ctf OCA], [http://pdbe.org/6ctf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ctf RCSB], [http://www.ebi.ac.uk/pdbsum/6ctf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ctf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://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]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Boudker, O]]
+[[Category: Oh, S]]
+[[Category: Ligand-bound]]
+[[Category: Membrane protein]]
+[[Category: Transporter]]