Structure of paracrystalline arrays on outer membranes of rat-liver and rat-heart mitochondria

Mannella, Carmen A.; Ribeiro, Alexandre J. S.; Cognon, B.; D'Arcangelis, D.

doi:10.1016/1047-8477(92)90023-4

Cited by 8 publications

(1 citation statement)

References 24 publications

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“…3 nm in diameter and 4.5 nm in height with a quaternary oligomerization state of six molecules in natural membranes. However, this approach could only be used to approximate the number of βstrands forming the underlying architecture [14,[31][32][33][34]. On the basis of bioinformatic and antibody epitope studies of VDAC proteins several two-dimensional models have been generated and 12-19 β-strands were predicted with model-dependent localization of the N-terminal helix either as part of or outside the barrel [35][36][37][38][39].…”

Section: Introductionmentioning

confidence: 99%

Porins in prokaryotes and eukaryotes: common themes and variations

Zeth

Thein

2010

Biochemical Journal

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Gram-negative bacteria and mitochondria are both covered by two distinct biological membranes. These membrane systems have been maintained during the course of evolution from an early evolutionary precursor. Both outer membranes accommodate channels of the porin family, which are designed for the uptake and exchange of metabolites, including ions and small molecules, such as nucleosides or sugars. In bacteria, the structure of the outer membrane porin protein family of β-barrels is generally characterized by an even number of β-strands; usually 14, 16 or 18 strands are observed forming the bacterial porin barrel wall. In contrast, the recent structures of the mitochondrial porin, also known as VDAC (voltage-dependent anion channel), show an uneven number of 19 β-strands, but a similar molecular architecture. Despite the lack of a clear evolutionary link between these protein families, their common principles and differences in assembly, architecture and function are summarized in the present review.

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Section: Introductionmentioning

confidence: 99%

Porins in prokaryotes and eukaryotes: common themes and variations

Zeth

Thein

2010

Biochemical Journal

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Mitochondrial Porins, Eukaryotic

Benz

2006

Encyclopedia of Molecular Cell Biology and Molecular Medicine

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From Channel‐Forming Ionic Liquid Crystals Exhibiting Humidity‐Induced Phase Transitions to Nanostructured Ion‐Conducting Polymer Membranes

Zhang

Möller

et al. 2013

Advanced Materials

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A novel wedge-shaped amphiphilic molecule bearing a sulfonate group at the tip displays humidity-induced phase transitions from a hexagonal columnar structure to a bicontinuous cubic phase. The mesophases can be frozen by photopolymerization of acrylic end-groups resulting in free-standing membranes with different topology of ionic nanochannels. The obtained membranes with a well-ordered ionic channel structure hold promise for applications in separation and catalysis.

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Structure of paracrystalline arrays on outer membranes of rat-liver and rat-heart mitochondria

Cited by 8 publications

References 24 publications

Porins in prokaryotes and eukaryotes: common themes and variations

Porins in prokaryotes and eukaryotes: common themes and variations

Mitochondrial Porins, Eukaryotic

From Channel‐Forming Ionic Liquid Crystals Exhibiting Humidity‐Induced Phase Transitions to Nanostructured Ion‐Conducting Polymer Membranes

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