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0  structures 253  species 0  interactions 859  sequences 6  architectures

Family: Porin_3 (PF01459)

Summary: Eukaryotic porin

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This is the Wikipedia entry entitled "Voltage-dependent anion channel". More...

Voltage-dependent anion channel Edit Wikipedia article

Eukaryotic porin
Identifiers
Symbol Porin_3
Pfam PF01459
InterPro IPR001925
PROSITE PDOC00483
TCDB 1.B.8
OPM family 210
OPM protein 3emn
CDD cd07306

Voltage-dependent anion channels are a class of porin ion channel located on the outer mitochondrial membrane.[1]

This major protein of the outer mitochondrial membrane of eukaryotes. It forms a voltage-dependent anion-selective channel (VDAC) that behaves as a general diffusion pore for small hydrophilic molecules.[2][3][4][5] The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. VDAC facilitates the exchange of ions and molecules between mitochondria and cytosol and is regulated by the interactions with other proteins and small molecules.[6]

Contents

[edit] Structure

This protein contains about 280 amino acids and its sequence is composed of between 12 to 16 beta-strands that span the mitochondrial outer membrane.[7]

Since its discovery in 1976, extensive function and structure analysis of VDAC proteins has been conducted. A prominent feature of the pore emerged: when reconstituted into planar lipid bilayers, there is a voltage-dependent switch between an anion-selective high-conductance state with high metabolite flux and a cation-selective low-conductance state with limited passage of metabolites.

More than 30 years after its initial discovery, in 2008, three independent structural projects of VDAC-1 were completed. The first was solved by multi-dimensional NMR spectroscopy. The second applied a hybrid approach using crystallographic data. The third was for mouse VDAC-1 crystals determined by X-ray crystallographic techniques. The three projects of the 3D structures of VDAC-1 revealed many structural features. First, VDAC-1 represents a new structural class of outer membrane β-barrel proteins with an odd number of strands. Another aspect is that the negatively charged side chain of residue E73 is oriented towards the hydrophobic membrane environment. The 19-stranded 3D structure obtained under different experimental sources by three different laboratories fits the EM and AFM data from native membrane sources and represents a biologically relevant state of VDAC-1.[6]

[edit] Examples

Yeast contains two members of this family (genes POR1 and POR2); vertebrates have at least three members (genes VDAC1, VDAC2 and VDAC3).[7]

Human proteins containing this domain include TOMM40, TOMM40L, VDAC1, VDAC2, and VDAC3.

[edit] References

  1. ^ Hoogenboom BW, Suda K, Engel A, Fotiadis D (2007). "The supramolecular assemblies of voltage-dependent anion channels in the native membrane". J. Mol. Biol. 370 (2): 246–55. doi:10.1016/j.jmb.2007.04.073. PMID 17524423. 
  2. ^ Benz R (1994). "Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins". Biochim. Biophys. Acta 1197 (2): 167–196. PMID 8031826. 
  3. ^ Mannella CA (1992). "The 'ins' and 'outs' of mitochondrial membrane channels". Trends Biochem. Sci. 17 (8): 315–320. doi:10.1016/0968-0004(92)90444-E. PMID 1384178. 
  4. ^ Dihanich M (1990). "The biogenesis and function of eukaryotic porins". Experientia 46 (2): 146–153. doi:10.1007/BF02027310. PMID 1689252. 
  5. ^ Forte M, Guy HR, Mannella CA (1987). "Molecular genetics of the VDAC ion channel: structural model and sequence analysis". J. Bioenerg. Biomembr. 19 (4): 341–350. doi:10.1007/BF00768537. PMID 2442148. 
  6. ^ a b Hiller S, Abramson J, Mannella C, Wagner G, Zeth K (September 2010). "The 3D structures of VDAC represent a native conformation". Trends Biochem. Sci. 35 (9): 514–21. doi:10.1016/j.tibs.2010.03.005. PMC 2933295. PMID 20708406. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2933295. 
  7. ^ a b Sampson MJ, Lovell RS, Davison DB, Craigen WJ (1996). "A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8". Genomics 36 (1): 192–196. doi:10.1006/geno.1996.0445. PMID 8812436. 

[edit] External links


This article incorporates text from the public domain Pfam and InterPro IPR001925

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Eukaryotic porin

No Pfam abstract.


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001925

The major protein of the outer mitochondrial membrane of eukaryotes is a porin that forms a voltage-dependent anion-selective channel (VDAC) that behaves as a general diffusion pore for small hydrophilic molecules [PUBMED:8031826, PUBMED:1384178, PUBMED:1689252, PUBMED:2442148]. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV.

This protein contains about 280 amino acids and its sequence is composed of between 12 to 16 beta-strands that span the mitochondrial outer membrane. Yeast contains two members of this family (genes POR1 and POR2); vertebrates have at least three members (genes VDAC1, VDAC2 and VDAC3) [PUBMED:8812436].

Gene Ontology

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Domain organisation

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Alignments

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The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

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Curation and family details

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Seed source: Prodom_3211 (release 99.1) & Pfam-B__3211 (release 7.5)
Previous IDs: Euk_porin;
Type: Family
Author: Bateman A
Number in seed: 92
Number in full: 859
Average length of the domain: 254.50 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 86.69 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 26.7 26.7
Trusted cut-off 26.9 26.8
Noise cut-off 26.6 26.6
Model length: 273
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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