Published in
Elsevier, Journal of Biological Chemistry, 18(289), p. 12566-12577, 2014
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- Elsevier
- [www.ncbi.nlm.nih.gov] | PDF
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- [europepmc.org] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
- [www.researchgate.net] | PDF
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High Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage-dependent Anion Channel 2 Reveal an Oligomeric Population*
,
Aviv Paz,
Carlos J. López,
Christian Altenbach ,
Calvin S. Leung,
Maria K. Drexler,
Jau-Nian Chen,
Wayne L. Hubbell,
Jeff Abramson
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Abstract
In recent years, there has been a vast increase in structural and functional understanding of VDAC1, but VDAC2 and 3 have been understudied despite having many unique phenotypes. One reason for the paucity of structural and biochemical characterization of the 2 and 3 isoforms stems from the inability of obtaining purified, functional protein. Here we demonstrate the expression, isolation, and basic characterization of zebrafish (zf) VDAC2. Further, we resolved the structure of zfVDAC2 at 2.8Å resolution revealing a crystallographic dimer. The dimer orientation was confirmed in solution by double electron-electron resonance spectroscopy and by cross-linking experiments disclosing a dimer population of ~20% in LDAO detergent micelles and ~40% in lipidic bicelles with the presence of some higher order oligomers in the latter. The present study allows for a more accurate structural comparison between VDAC2 and its better-studied counterpart VDAC1.