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Nature of In-Plane Phase Transitions in 2D Crystals of the Mitochondrial Porin, VDAC

Published online by Cambridge University Press:  02 July 2020

C.A. Mannella
C.A. Mannella*
Affiliation:
Biological Microscopy and Image Reconstruction Resource, Wadsworth Center, New York State Department of Health, Empire State Plaza, Box 509, Albany, NY, 12201-0509, and Department of Biomedical Sciences, School of Public Health, University at Albany (SUNY)
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Extract

VDAC is a voltage-gated ion and metabolite channel that occurs at high density in the mitochondrial outer membrane. Although VDAC is probably related structurally to bacterial porins, small transmembrane voltages cause it to undergo reversible, partial closures that are not seen with the prokaryotic pores. The “closed” states, which are impermeable to ATP, can be induced by effectors, including a synthetic polyanion. There is evidence that closure involves major rearrangements of the pore structure that are difficult to explain in terms of porin-like β-barrels.

The main source of information about the structure of VDAC is electron microscopy of 2D crystals obtained by phospholipase treatment of outer membranes of fungal mitochondria. The unit cell observed after partial lipid hydrolysis (a = 13.3 nm, b = 11.5 nm, γ = 109°) contains six pores which appear to be structurally equivalent at the resolution of correlation averages of crystals embedded in aurothioglucose or vitreous ice (∼1/1.5 nm−1).

Type
Electron Crystallography; the Electron Phase Problem
Information
Microscopy and Microanalysis , Volume 3 , Issue S2: Proceedings: Microscopy & Microanalysis '97, Microscopy Society of America 55th Annual Meeting, Microbeam Analysis Society 31st Annual Meeting, Histochemical Society 48th Annual Meeting, Cleveland, Ohio, August 10-14, 1997 , August 1997 , pp. 1065 - 1066
Copyright
Copyright © Microscopy Society of America 1997

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References

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