4BUM

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

4BUM の概要

• エントリーDOI: 10.2210/pdb4bum/pdb
• 分子名称: VOLTAGE-DEPENDENT ANION CHANNEL 2, LAURYL DIMETHYLAMINE-N-OXIDE (3 entities in total)
• 機能のキーワード: membrane protein, mitochondria, porin, membrane, detergent, recombinant
• 由来する生物種: DANIO RERIO (ZEBRAFISH)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31378.22

構造登録者

Paz, A.,Schredelseker, J.,Abramson, J. (登録日: 2013-06-21, 公開日: 2014-03-26, 最終更新日: 2023-12-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.801 Å)