6k5d - Revision history

OCA at 10:26, 22 November 2023

OCA — Wed, 22 Nov 2023 10:26:54 GMT

←Older revision		Revision as of 10:26, 22 November 2023
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	<StructureSection load='6k5d' size='340' side='right'caption='[[6k5d]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='6k5d' size='340' side='right'caption='[[6k5d]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6k5d]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K5D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6K5D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6k5d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K5D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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]] 3.203Å</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=6k5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k5d OCA], [~~http~~://pdbe.org/6k5d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6k5d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6k5d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6k5d ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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=6k5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k5d OCA], [https://pdbe.org/6k5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k5d RCSB], [https://www.ebi.ac.uk/pdbsum/6k5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k5d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~J7Q633_ECOLX J7Q633_ECOLX~~]~~] Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.[SAAS:SAAS00552659]~~ Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.~~[HAMAP-Rule~~:~~MF_01128][SAAS~~:~~SAAS00010056]~~	+	[https://www.uniprot.org/uniprot/CLCA_ECOLI CLCA_ECOLI] Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.<ref>PMID:12384697</ref> <ref>PMID:14985752</ref> <ref>PMID:16341087</ref> <ref>PMID:16905147</ref> <ref>PMID:18678918</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 6k5d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6k5d" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ion channels 3D structures\|Ion channels 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lim, H H~~]]	+	[[Category: Mus musculus]]
-	[[Category: ~~Park, K~~]]	+	[[Category: Lim HH]]
-	[[Category: ~~Cl- / h+ antiporter]]~~	+	[[Category: Park K]]
-	~~[[Category: Clc transporter]]~~	+
-	~~[[Category: Membrane protein~~]]	+

OCA at 15:29, 28 August 2019

OCA — Wed, 28 Aug 2019 15:29:13 GMT

←Older revision		Revision as of 15:29, 28 August 2019
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-	'''Unreleased structure'''

-	~~The entry~~ 6k5d is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of the E148N mutant CLC-ec1 in presence of 200 mM NaBr==
		+	<StructureSection load='6k5d' size='340' side='right'caption='[[6k5d]], [[Resolution\|resolution]] 3.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6k5d]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K5D FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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=6k5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k5d OCA], [http://pdbe.org/6k5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k5d RCSB], [http://www.ebi.ac.uk/pdbsum/6k5d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k5d ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/J7Q633_ECOLX J7Q633_ECOLX]] Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.[SAAS:SAAS00552659] Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.[HAMAP-Rule:MF_01128][SAAS:SAAS00010056]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The CLC family of proteins are involved in a variety of physiological processes to control cellular chloride concentration. Two distinct classes of CLC proteins, Cl(-) channels and Cl(-)/H(+) antiporters, have been functionally and structurally investigated over the last several decades. Previous studies have suggested that the conformational heterogeneity of the critical glutamate residue, Gluex, could explain the transport cycle of CLC-type Cl(-)/H(+) antiporters. However, the presence of multiple conformations (Up, Middle, and Down) of the Gluex has been suggested from combined structural snapshots of 2 different CLC antiporters: CLC-ec1 from Escherichia coli and cmCLC from a thermophilic red alga, Cyanidioschyzon merolae Thus, we aimed to investigate further the heterogeneity of Gluex-conformations in CLC-ec1, the most deeply studied CLC antiporter, at both functional and structural levels. Here, we show that the crystal structures of the Gluex mutant E148D and wild-type CLC-ec1 with varying anion concentrations suggest a structural intermediate, the "Midlow" conformation. We also found that an extra anion can be located above the external Cl(-)-binding site in the E148D mutant when the anion concentration is high. Moreover, we observed that a carboxylate in solution can occupy either the external or central Cl(-)-binding site in the ungated E148A mutant using an anomalously detectable short carboxylic acid, bromoacetate. These results lend credibility to the idea that the Gluex can take at least 3 distinct conformational states during the transport cycle of a single CLC antiporter.

-	~~Authors~~:	+	Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC Cl(-)/H(+) antiporter.,Park K, Lee BC, Lim HH Proc Natl Acad Sci U S A. 2019 Aug 13. pii: 1901822116. doi:, 10.1073/pnas.1901822116. PMID:31409705<ref>PMID:31409705</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6k5d" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Lim, H H]]
		+	[[Category: Park, K]]
		+	[[Category: Cl- / h+ antiporter]]
		+	[[Category: Clc transporter]]
		+	[[Category: Membrane protein]]

OCA at 05:03, 26 June 2019

OCA — Wed, 26 Jun 2019 05:03:42 GMT

←Older revision		Revision as of 05:03, 26 June 2019
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6k5d is ON HOLD	+	The entry 6k5d is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6k5d" [edit=sysop:move=sysop]

OCA — Wed, 05 Jun 2019 21:01:21 GMT

Protected "6k5d" [edit=sysop:move=sysop]

←Older revision

Revision as of 21:01, 5 June 2019

OCA: New page: '''Unreleased structure''' The entry 6k5d is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 05 Jun 2019 21:01:20 GMT

New page: '''Unreleased structure''' The entry 6k5d is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6k5d is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]