Structure and function of the porin channel

Welte, Wolfram; Nestel, Uwe; Wacker, Thomas; Diederichs, Kay

doi:10.1038/ki.1995.374

Cited by 59 publications

(44 citation statements)

References 119 publications

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“…tive potentials, where VDAC closure is associated with motion of the positively-charged voltage sensor [19,34]. It has been postulated that a positively charged loop moves out of the channel [34], but it is also possible that negative charges move into the mouth of the channel, as has been observed for bacterial porins [35]. Thus, the molecular nature of the VDAC gating mechanism is not yet resolved.…”

Section: Vdac Conductance Voltage Dependence and Ion Selectivitymentioning

confidence: 96%

The Voltage-Dependent Anion Channel (VDAC): Function in Intracellular Signalling, Cell Life and Cell Death

Shoshan‐Barmatz

Israelson²,

Brdiczka³

et al. 2006

CPD

285

329

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Research over the last decade has extended the prevailing view of mitochondria to include functions well beyond the critical bioenergetics role in supplying ATP. It is now recognized that mitochondria play a crucial role in cell signaling events, inter-organelle communication, aging, many diseases, cell proliferation and cell death. Apoptotic signal transmission to the mitochondria results in the efflux of a number of potential apoptotic regulators to the cytosol that trigger caspase activation and lead to cell destruction. Accumulating evidence indicates that the voltage-dependent anion channel (VDAC) is involved in this release of proteins via the outer mitochondrial membrane. VDAC in the outer mitochondrial membrane is in a crucial position in the cell, forming the main interface between the mitochondrial and the cellular metabolisms. VDAC has been recognized as a key protein in mitochondria-mediated apoptosis since it is the proposed target for the pro- and anti-apoptotic Bcl2-family of proteins and due to its function in the release of apoptotic proteins located in the inter-membranal space. The diameter of the VDAC pore is only about 2.6-3 nm, which is insufficient for passage of a folded protein like cytochrome c. New work suggests pore formation by homo-oligomers of VDAC or hetero-oligomers composed of VDAC and pro-apoptotic proteins such as Bax or Bak. This review provides insights into the central role of VDAC in cell life and death and emphasizes its function in the regulation of mitochondria-mediated apoptosis and, thereby, its potential as a rational target for new therapeutics.

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Section: Vdac Conductance Voltage Dependence and Ion Selectivitymentioning

confidence: 96%

The Voltage-Dependent Anion Channel (VDAC): Function in Intracellular Signalling, Cell Life and Cell Death

Shoshan‐Barmatz

Israelson²,

Brdiczka³

et al. 2006

CPD

285

329

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“…They form weakly ion-selective channels for small hydrophilic molecules with size-exclusion limits around 600 Da [1,2]. Porins form stable homotrimers that are resistant to detergents and proteases.…”

Section: Introductionmentioning

confidence: 99%

The structure of porin from Paracoccus denitrificans at 3.1 Å resolution

et al. 1997

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The crystal structure of a non-specific porin from Paracoccus denitrificans at 3.1 A resolution has been solved by molecular replacement using the porin from Rhodopseudomonas blastica as the search model. Paracoccus porin is very similar to other non-specific porins of known structure: a trimer of 16 stranded P-barrels each with a central pore constricted by a long extracellular loop folding back against the barrel wall. The distinctive distribution of charged residues of this non-specific porin contributes to understanding the relation between structure and ion selectivity.

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“…Eight loops connect neighbouring strands at the extraplasmic surface while seven or eight short hairpin turns are found at the periplasmic surface. The typical exclusion limit for nonspeci®c porins was estimated to be $600 Da (Nikaido & Vaara, 1985;Welte et al, 1995) and is mainly controlled by the size of the pore constriction zone formed by loop 3 folding back into the pore. The structural conditions of functional properties concerning the passage of ions (i.e.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray crystallographic studies of the native and chemically modified anion-selective porin fromComamonas acidovorans

et al. 1998

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Omp32, the strongly anion-selective porin from Comamonas acidovorans, has been crystallized. Two crystal forms were observed, both of which belong to space group R3, but exhibit different cell dimensions a = b = 106.7, c = 140.6 A Ê (crystal form I) and a = b = 87.1, c = 135.3 A Ê (crystal form II) with one trimer per asymmetric unit. The crystals diffract to 2.2 and 2.3 A Ê resolution, respectively. Omp32 was chemically modi®ed by introducing negative charges through succinylation. The number and positions of the individual modi®cations were determined using mass spectrometry and X-ray crystallography. Chemically modi®ed porins yielded crystals of a third form, also of space group R3 but with cell constants of a = b = 109.3 and c = 263.2 A Ê (crystal form III), showing a virtually doubled c axis. Crystals of form III diffract to 3.5 A Ê resolution.

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Structure and function of the porin channel

Cited by 59 publications

References 119 publications

The Voltage-Dependent Anion Channel (VDAC): Function in Intracellular Signalling, Cell Life and Cell Death

The Voltage-Dependent Anion Channel (VDAC): Function in Intracellular Signalling, Cell Life and Cell Death

The structure of porin from Paracoccus denitrificans at 3.1 Å resolution

Crystallization and preliminary X-ray crystallographic studies of the native and chemically modified anion-selective porin fromComamonas acidovorans

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