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3emn

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[[Image:3emn.png|left|200px]]
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==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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== 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/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>
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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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<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>
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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://www.rcsb.org/pdb/explore.do?structureId=3emn RCSB], [http://www.ebi.ac.uk/pdbsum/3emn PDBsum]</span></td></tr>
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</table>
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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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{{STRUCTURE_3emn| PDB=3emn | SCENE= }}
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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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===The Crystal Structure of Mouse VDAC1 at 2.3 A resolution===
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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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{{ABSTRACT_PUBMED_18988731}}
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==About this Structure==
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[[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].
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==See Also==
==See Also==
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*[[Porin|Porin]]
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*[[Ion channels|Ion channels]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:018988731</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Abramson, J.]]
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[[Category: Abramson, J]]
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[[Category: Cascio, D.]]
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[[Category: Cascio, D]]
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[[Category: Colletier, J P.]]
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[[Category: Colletier, J P]]
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[[Category: Faham, S.]]
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[[Category: Faham, S]]
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[[Category: Ping, P.]]
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[[Category: Ping, P]]
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[[Category: Toro, L.]]
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[[Category: Toro, L]]
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[[Category: Ujwal, R.]]
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[[Category: Ujwal, R]]
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[[Category: Zhang, J.]]
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[[Category: Zhang, J]]
[[Category: Apoptosis]]
[[Category: Apoptosis]]
[[Category: Beta barrel]]
[[Category: Beta barrel]]

Revision as of 13:29, 19 November 2014

The Crystal Structure of Mouse VDAC1 at 2.3 A resolution

3emn, resolution 2.30Å

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