3emn: Difference between revisions

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<StructureSection load='3emn' size='340' side='right'caption='[[3emn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3emn' size='340' side='right'caption='[[3emn]], [[Resolution|resolution]] 2.30&Aring;' 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]] 2.3&#8491;</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 ==
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</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]]

Revision as of 18:58, 29 November 2023

The Crystal Structure of Mouse VDAC1 at 2.3 A resolution

3emn, resolution 2.30Å

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