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3emn

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Revision as of 06:11, 25 December 2014

The Crystal Structure of Mouse VDAC1 at 2.3 A resolution

Structural highlights

3emn is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Vdac1, Vdac5 (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Buettner R, Papoutsoglou G, Scemes E, Spray DC, Dermietzel R. Evidence for secretory pathway localization of a voltage-dependent anion channel isoform. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3201-6. PMID:10716730 doi:http://dx.doi.org/10.1073/pnas.060242297
↑ Okada SF, O'Neal WK, Huang P, Nicholas RA, Ostrowski LE, Craigen WJ, Lazarowski ER, Boucher RC. Voltage-dependent anion channel-1 (VDAC-1) contributes to ATP release and cell volume regulation in murine cells. J Gen Physiol. 2004 Nov;124(5):513-26. Epub 2004 Oct 11. PMID:15477379 doi:http://dx.doi.org/jgp.200409154
↑ Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J. The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17742-7. Epub 2008 Nov 6. PMID:18988731 doi:0809634105
↑ Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, Abramson J. The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17742-7. Epub 2008 Nov 6. PMID:18988731 doi:0809634105

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3emn"

@@ 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>
 </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;">
 == Publication Abstract from PubMed ==

3emn

From Proteopedia

Revision as of 06:11, 25 December 2014

The Crystal Structure of Mouse VDAC1 at 2.3 A resolution

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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