6ctf - Revision history

OCA at 15:10, 4 October 2023

OCA — Wed, 04 Oct 2023 15:10:49 GMT

←Older revision		Revision as of 15:10, 4 October 2023
Line 1:		Line 1:

	==Crystal structure of GltPh fast mutant - R276S/M395R==		==Crystal structure of GltPh fast mutant - R276S/M395R==
-	<StructureSection load='6ctf' size='340' side='right' caption='[[6ctf]], [[Resolution\|resolution]] 4.05Å' scene=''>	+	<StructureSection load='6ctf' size='340' side='right'caption='[[6ctf]], [[Resolution\|resolution]] 4.05Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6ctf]] 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=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>	+	<table><tr><td colspan='2'>[[6ctf]] 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=6CTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CTF FirstGlance]. <br>
-	</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>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 4.05Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~PH1295 ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=70601 Pyrococcus horikoshii])~~</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<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>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ctf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ctf OCA], [https://pdbe.org/6ctf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ctf RCSB], [https://www.ebi.ac.uk/pdbsum/6ctf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ctf ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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]	+	[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]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 6ctf" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6ctf" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Symporter 3D structures\|Symporter 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Pyrococcus horikoshii~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Boudker, O~~]]	+	[[Category: Pyrococcus horikoshii OT3]]
-	[[Category: ~~Oh, S~~]]	+	[[Category: Boudker O]]
-	[[Category: ~~Ligand-bound]]~~	+	[[Category: Oh S]]
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Transporter~~]]	+

OCA at 07:12, 31 October 2018

OCA — Wed, 31 Oct 2018 07:12:01 GMT

←Older revision		Revision as of 07:12, 31 October 2018
Line 3:		Line 3:
	<StructureSection load='6ctf' size='340' side='right' caption='[[6ctf]], [[Resolution\|resolution]] 4.05Å' scene=''>		<StructureSection load='6ctf' size='340' side='right' caption='[[6ctf]], [[Resolution\|resolution]] 4.05Å' scene=''>
	== Structural highlights ==		== 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>	+	<table><tr><td colspan='2'>[[6ctf]] 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=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>
	</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>		</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>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PH1295 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</td></tr>
	<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>		<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>		</table>
	== Function ==		== 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]		[[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]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Many secondary active membrane transporters pump substrates against concentration gradients by coupling their uptake to symport of sodium ions. Symport requires the substrate and ions to be always transported together. Cooperative binding of the solutes is a key mechanism contributing to coupled transport in the sodium and aspartate symporter from Pyrococcus horikoshii GltPh. Here, we describe the kinetic mechanism of coupled binding for GltPh in the inward facing state. The first of the three coupled sodium ions, binds weakly and slowly, enabling the protein to accept the rest of the ions and the substrate. The last ion binds tightly, but is in rapid equilibrium with solution. Its release is required for the complex disassembly. Thus, the first ion serves to 'open the door' for the substrate, the last ion 'locks the door' once the substrate is in, and one ion contributes to both events.
		+
		+	Kinetic mechanism of coupled binding in sodium-aspartate symporter GltPh.,Oh S, Boudker O Elife. 2018 Sep 26;7. pii: 37291. doi: 10.7554/eLife.37291. PMID:30255846<ref>PMID:30255846</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6ctf" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Pyrococcus horikoshii]]
	[[Category: Boudker, O]]		[[Category: Boudker, O]]
	[[Category: Oh, S]]		[[Category: Oh, S]]

OCA at 08:05, 10 October 2018

OCA — Wed, 10 Oct 2018 08:05:13 GMT

←Older revision		Revision as of 08:05, 10 October 2018
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]] 4.05Å' 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]]

OCA at 03:58, 30 May 2018

OCA — Wed, 30 May 2018 03:58:57 GMT

←Older revision		Revision as of 03:58, 30 May 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6ctf is ON HOLD	+	The entry 6ctf is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6ctf" [edit=sysop:move=sysop]

OCA — Wed, 28 Mar 2018 05:23:40 GMT

Protected "6ctf" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:23, 28 March 2018

OCA: New page: '''Unreleased structure''' The entry 6ctf is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 28 Mar 2018 05:23:38 GMT

New page: '''Unreleased structure''' The entry 6ctf is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6ctf is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]