4BUM

Crystal structure of the Voltage Dependant Anion Channel 2 from zebrafish.

Summary for 4BUM

• Entry DOI: 10.2210/pdb4bum/pdb
• Descriptor: VOLTAGE-DEPENDENT ANION CHANNEL 2, LAURYL DIMETHYLAMINE-N-OXIDE (3 entities in total)
• Functional Keywords: membrane protein, mitochondria, porin, membrane, detergent, recombinant
• Biological source: DANIO RERIO (ZEBRAFISH)
• Total number of polymer chains: 1
• Total formula weight: 31378.22

Authors

Paz, A.,Schredelseker, J.,Abramson, J. (deposition date: 2013-06-21, release date: 2014-03-26, Last modification date: 2023-12-20)

Primary citation

Schredelseker, J.,Paz, A.,Lopez, C.J.,Altenbach, C.,Leung, C.S.,Drexler, M.K.,Chen, J.,Hubbell, W.L.,Abramson, J.
High-Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage Dependent Anion Channel 2 Reveal an Oligomeric Population.
J.Biol.Chem., 289:12566-, 2014

PubMed 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 VDAC2 and -3 isoforms stems from the inability of obtaining purified, functional protein. Here we demonstrate the expression, isolation, and basic characterization of zebrafish VDAC2 (zfVDAC2). Further, we resolved the structure of zfVDAC2 at 2.8 Å 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 lauryldimethine amine oxide detergent micelles, whereas in lipidic bicelles a higher population of dimeric and higher order oligomers species were observed. The present study allows for a more accurate structural comparison between VDAC2 and its better-studied counterpart VDAC1.

PubMed: 24627492
DOI: 10.1074/JBC.M113.497438

Experimental method

X-RAY DIFFRACTION (2.801 Å)