3emn

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==The Crystal Structure of Mouse VDAC1 at 2.3 A resolution==
==The Crystal Structure of Mouse VDAC1 at 2.3 A resolution==
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<StructureSection load='3emn' size='340' side='right' caption='[[3emn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='3emn' size='340' side='right'caption='[[3emn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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>
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<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>
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<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>
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<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 ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3emn" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Ion channels|Ion channels]]
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*[[Ion channels 3D structures|Ion channels 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Abramson, J]]
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[[Category: Mus musculus]]
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[[Category: Cascio, D]]
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[[Category: Abramson J]]
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[[Category: Colletier, J P]]
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[[Category: Cascio D]]
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[[Category: Faham, S]]
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[[Category: Colletier J-P]]
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[[Category: Ping, P]]
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[[Category: Faham S]]
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[[Category: Toro, L]]
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[[Category: Ping P]]
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[[Category: Ujwal, R]]
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[[Category: Toro L]]
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[[Category: Zhang, J]]
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[[Category: Ujwal R]]
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[[Category: Apoptosis]]
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[[Category: Zhang J]]
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[[Category: Beta barrel]]
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[[Category: Channel]]
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[[Category: Eukaryotic membrane protein]]
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[[Category: Ion transport]]
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[[Category: Membrane protein]]
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[[Category: Mitochondrion]]
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[[Category: Outer membrane]]
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[[Category: Phosphoprotein]]
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[[Category: Porin]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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[[Category: Vdac1]]
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Current revision

The Crystal Structure of Mouse VDAC1 at 2.3 A resolution

PDB ID 3emn

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