3emn - Revision history

OCA at 09:48, 21 February 2024

OCA — Wed, 21 Feb 2024 09:48:19 GMT

←Older revision		Revision as of 09:48, 21 February 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/VDAC1_MOUSE VDAC1_MOUSE] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:10716730</ref> <ref>PMID:15477379</ref> <ref>PMID:18988731</ref>		[https://www.uniprot.org/uniprot/VDAC1_MOUSE VDAC1_MOUSE] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:10716730</ref> <ref>PMID:15477379</ref> <ref>PMID:18988731</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The voltage-dependent anion channel (VDAC) constitutes the major pathway for the entry and exit of metabolites across the outer membrane of the mitochondria and can serve as a scaffold for molecules that modulate the organelle. We report the crystal structure of a beta-barrel eukaryotic membrane protein, the murine VDAC1 (mVDAC1) at 2.3 A resolution, revealing a high-resolution image of its architecture formed by 19 beta-strands. Unlike the recent NMR structure of human VDAC1, the position of the voltage-sensing N-terminal segment is clearly resolved. The alpha-helix of the N-terminal segment is oriented against the interior wall, causing a partial narrowing at the center of the pore. This segment is ideally positioned to regulate the conductance of ions and metabolites passing through the VDAC pore.
-
-	The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating.,Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17742-7. Epub 2008 Nov 6. PMID:18988731<ref>PMID:18988731</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3emn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 18:58, 29 November 2023

OCA — Wed, 29 Nov 2023 18:58:06 GMT

←Older revision		Revision as of 18:58, 29 November 2023
Line 3:		Line 3:
	<StructureSection load='3emn' size='340' side='right'caption='[[3emn]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3emn' size='340' side='right'caption='[[3emn]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3emn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EMN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3emn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EMN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MC3:1~~,2~~-DIMYRISTOYL-RAC-GLYCERO-~~3~~-PHOSPHOCHOLINE'>MC3</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]] 2.3Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~Vdac1~~, ~~Vdac5 ([https:~~/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [https://pdbe.org/3emn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [https://www.ebi.ac.uk/pdbsum/3emn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3emn 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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [https://pdbe.org/3emn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [https://www.ebi.ac.uk/pdbsum/3emn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3emn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/VDAC1_MOUSE VDAC1_MOUSE]] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:10716730</ref> <ref>PMID:15477379</ref> <ref>PMID:18988731</ref>	+	[https://www.uniprot.org/uniprot/VDAC1_MOUSE VDAC1_MOUSE] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:10716730</ref> <ref>PMID:15477379</ref> <ref>PMID:18988731</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Abramson, J]]	+	[[Category: Abramson J]]
-	[[Category: Cascio, D]]	+	[[Category: Cascio D]]
-	[[Category: Colletier, J P]]	+	[[Category: Colletier J-P]]
-	[[Category: Faham, S]]	+	[[Category: Faham S]]
-	[[Category: Ping, P]]	+	[[Category: Ping P]]
-	[[Category: Toro, L]]	+	[[Category: Toro L]]
-	[[Category: Ujwal, R]]	+	[[Category: Ujwal R]]
-	[[Category: Zhang, J]]	+	[[Category: Zhang J]]
-	~~[[Category: Apoptosis]]~~	+
-	~~[[Category: Beta barrel]]~~	+
-	~~[[Category: Channel]]~~	+
-	~~[[Category: Eukaryotic membrane protein]]~~	+
-	~~[[Category: Ion transport]]~~	+
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Mitochondrion]]~~	+
-	~~[[Category: Outer membrane]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Porin]]~~	+
-	~~[[Category: Transmembrane]]~~	+
-	~~[[Category: Transport]]~~	+
-	~~[[Category: Vdac1~~]]	+

OCA at 09:10, 23 February 2022

OCA — Wed, 23 Feb 2022 09:10:06 GMT

←Older revision		Revision as of 09:10, 23 February 2022
Line 1:		Line 1:

	==The Crystal Structure of Mouse VDAC1 at 2.3 A resolution==		==The Crystal Structure of Mouse VDAC1 at 2.3 A resolution==
-	<StructureSection load='3emn' size='340' side='right' caption='[[3emn]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='3emn' size='340' side='right'caption='[[3emn]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3emn]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EMN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3emn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EMN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Vdac1, Vdac5 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Vdac1, Vdac5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [~~http~~://pdbe.org/3emn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3emn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3emn 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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [https://pdbe.org/3emn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [https://www.ebi.ac.uk/pdbsum/3emn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3emn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/VDAC1_MOUSE VDAC1_MOUSE]] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:10716730</ref> <ref>PMID:15477379</ref> <ref>PMID:18988731</ref>	+	[[https://www.uniprot.org/uniprot/VDAC1_MOUSE VDAC1_MOUSE]] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:10716730</ref> <ref>PMID:15477379</ref> <ref>PMID:18988731</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:

	==See Also==		==See Also==
-	*[[Ion channels\|Ion channels]]	+	*[[Ion channels 3D structures\|Ion channels 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Abramson, J]]		[[Category: Abramson, J]]

OCA at 21:58, 5 August 2016

OCA — Fri, 05 Aug 2016 21:58:25 GMT

←Older revision		Revision as of 21:58, 5 August 2016
Line 1:		Line 1:
		+
	==The Crystal Structure of Mouse VDAC1 at 2.3 A resolution==		==The Crystal Structure of Mouse VDAC1 at 2.3 A resolution==
	<StructureSection load='3emn' size='340' side='right' caption='[[3emn]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3emn' size='340' side='right' caption='[[3emn]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3emn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EMN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3emn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EMN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Vdac1, Vdac5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Vdac1, Vdac5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [http://www.ebi.ac.uk/pdbsum/3emn PDBsum]</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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [http://pdbe.org/3emn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [http://www.ebi.ac.uk/pdbsum/3emn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3emn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3emn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Abramson, J]]		[[Category: Abramson, J]]
	[[Category: Cascio, D]]		[[Category: Cascio, D]]

OCA at 06:11, 25 December 2014

OCA — Thu, 25 Dec 2014 06:11:02 GMT

←Older revision		Revision as of 06:11, 25 December 2014
Line 7:		Line 7:
	<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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [http://www.ebi.ac.uk/pdbsum/3emn PDBsum]</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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [http://www.ebi.ac.uk/pdbsum/3emn PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/VDAC1_MOUSE VDAC1_MOUSE]] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:10716730</ref> <ref>PMID:15477379</ref> <ref>PMID:18988731</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 13:29, 19 November 2014

OCA — Wed, 19 Nov 2014 13:29:04 GMT

←Older revision		Revision as of 13:29, 19 November 2014
Line 1:		Line 1:
-	[[~~Image:~~3emn.~~png~~\|~~left~~\|~~200px~~]]	+	==The Crystal Structure of Mouse VDAC1 at 2.3 A resolution==
		+	<StructureSection load='3emn' size='340' side='right' caption='[[3emn]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3emn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EMN FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Vdac1, Vdac5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3emn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3emn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [http://www.ebi.ac.uk/pdbsum/3emn PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The voltage-dependent anion channel (VDAC) constitutes the major pathway for the entry and exit of metabolites across the outer membrane of the mitochondria and can serve as a scaffold for molecules that modulate the organelle. We report the crystal structure of a beta-barrel eukaryotic membrane protein, the murine VDAC1 (mVDAC1) at 2.3 A resolution, revealing a high-resolution image of its architecture formed by 19 beta-strands. Unlike the recent NMR structure of human VDAC1, the position of the voltage-sensing N-terminal segment is clearly resolved. The alpha-helix of the N-terminal segment is oriented against the interior wall, causing a partial narrowing at the center of the pore. This segment is ideally positioned to regulate the conductance of ions and metabolites passing through the VDAC pore.

-	~~{{STRUCTURE_3emn\| PDB=3emn \| SCENE= }}~~	+	The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating.,Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17742-7. Epub 2008 Nov 6. PMID:18988731<ref>PMID:18988731</ref>

-	~~===The Crystal Structure~~ of ~~Mouse VDAC1 at 2~~.~~3 A resolution===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18988731}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3emn]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA].~~	+

	==See Also==		==See Also==
-	*[[~~Porin~~\|~~Porin~~]]	+	*[[Ion channels\|Ion channels]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:018988731<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Abramson, J.]]	+	[[Category: Abramson, J]]
-	[[Category: Cascio, D.]]	+	[[Category: Cascio, D]]
-	[[Category: Colletier, J P.]]	+	[[Category: Colletier, J P]]
-	[[Category: Faham, S.]]	+	[[Category: Faham, S]]
-	[[Category: Ping, P.]]	+	[[Category: Ping, P]]
-	[[Category: Toro, L.]]	+	[[Category: Toro, L]]
-	[[Category: Ujwal, R.]]	+	[[Category: Ujwal, R]]
-	[[Category: Zhang, J.]]	+	[[Category: Zhang, J]]
	[[Category: Apoptosis]]		[[Category: Apoptosis]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]

OCA at 13:32, 20 October 2012

OCA — Sat, 20 Oct 2012 13:32:01 GMT

←Older revision		Revision as of 13:32, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3emn]] is a 1 chain structure ~~of [[Porin]]~~ with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA].	+	[[3emn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA].

	==See Also==		==See Also==

OCA: Protected "3emn" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 12:16:52 GMT

Protected "3emn" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:16, 26 July 2012

OCA at 12:16, 26 July 2012

OCA — Thu, 26 Jul 2012 12:16:50 GMT

←Older revision		Revision as of 12:16, 26 July 2012
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3emn.png\|left\|200px]]
-	[[Image:3emn.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3emn", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3emn\| PDB=3emn \| SCENE= }}		{{STRUCTURE_3emn\| PDB=3emn \| SCENE= }}

	===The Crystal Structure of Mouse VDAC1 at 2.3 A resolution===		===The Crystal Structure of Mouse VDAC1 at 2.3 A resolution===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18988731}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18988731 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18988731}}		{{ABSTRACT_PUBMED_18988731}}

	==About this Structure==		==About this Structure==
-	~~3EMN~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA].	+	[[3emn]] is a 1 chain structure of [[Porin]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA].
		+
		+	==See Also==
		+	*[[Porin\|Porin]]

	==Reference==		==Reference==
-	The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating., Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J, Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17742-7. Epub 2008 Nov 6. PMID:~~[http://www.ncbi.nlm.nih.gov~~/~~pubmed~~/~~18988731 18988731]~~	+	<ref group="xtra">PMID:018988731</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Abramson, J.]]		[[Category: Abramson, J.]]
Line 33:		Line 24:
	[[Category: Ujwal, R.]]		[[Category: Ujwal, R.]]
	[[Category: Zhang, J.]]		[[Category: Zhang, J.]]
-	[[Category: Acetylation]]
-	[[Category: Alternative splicing]]
	[[Category: Apoptosis]]		[[Category: Apoptosis]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]
Line 40:		Line 29:
	[[Category: Eukaryotic membrane protein]]		[[Category: Eukaryotic membrane protein]]
	[[Category: Ion transport]]		[[Category: Ion transport]]
		+	[[Category: Membrane protein]]
	[[Category: Mitochondrion]]		[[Category: Mitochondrion]]
	[[Category: Outer membrane]]		[[Category: Outer membrane]]
Line 47:		Line 37:
	[[Category: Transport]]		[[Category: Transport]]
	[[Category: Vdac1]]		[[Category: Vdac1]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 17 13:45:08 2008''

OCA at 11:45, 17 December 2008

OCA — Wed, 17 Dec 2008 11:45:10 GMT

←Older revision		Revision as of 11:45, 17 December 2008
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3emn.jpg\|left\|200px]]

-	The ~~entry 3emn~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3emn", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3emn\| PDB=3emn \| SCENE= }}

-	~~Authors: Ujwal, R., Cascio, D., Colletier, J.-P., Faham, S., Zhang, J., Toro, L., Ping, P., Abramson, J~~.	+	===The Crystal Structure of Mouse VDAC1 at 2.3 A resolution===

-	Description: The Crystal Structure of Mouse VDAC1 at 2.3 A resolution

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Nov 5 11~~:42:02 2008''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_18988731}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18988731 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18988731}}
		+
		+	==About this Structure==
		+	3EMN is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EMN OCA].
		+
		+	==Reference==
		+	The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating., Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J, Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17742-7. Epub 2008 Nov 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18988731 18988731]
		+	[[Category: Mus musculus]]
		+	[[Category: Abramson, J.]]
		+	[[Category: Cascio, D.]]
		+	[[Category: Colletier, J P.]]
		+	[[Category: Faham, S.]]
		+	[[Category: Ping, P.]]
		+	[[Category: Toro, L.]]
		+	[[Category: Ujwal, R.]]
		+	[[Category: Zhang, J.]]
		+	[[Category: Acetylation]]
		+	[[Category: Alternative splicing]]
		+	[[Category: Apoptosis]]
		+	[[Category: Beta barrel]]
		+	[[Category: Channel]]
		+	[[Category: Eukaryotic membrane protein]]
		+	[[Category: Ion transport]]
		+	[[Category: Mitochondrion]]
		+	[[Category: Outer membrane]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Porin]]
		+	[[Category: Transmembrane]]
		+	[[Category: Transport]]
		+	[[Category: Vdac1]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 17 13:45:08 2008''