Gattin Zrinka, Schneider Robert, Laukat Yvonne, Giller Karin, Maier Elke, Zweckstetter Markus, Griesinger Christian, Benz Roland, Becker Stefan, Lange Adam
Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
J Biomol NMR. 2015 Apr;61(3-4):311-20. doi: 10.1007/s10858-014-9876-5. Epub 2014 Nov 16.
The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the structure of hVDAC1, in line with recent investigations on zfVDAC2. However, hVDAC2 appears to exhibit an increased conformational heterogeneity compared to hVDAC1 which is reflected in broader solid-state NMR spectra and less defined electrophysiological profiles.
电压依赖性阴离子通道(VDAC)是线粒体外膜中含量最丰富的蛋白质,构成了ADP、ATP和其他代谢物运输的主要途径。在这项多学科研究中,我们结合了固态核磁共振、电生理学和分子动力学模拟,以研究脂质双层环境中人类VDAC同工型2的结构。我们发现,hVDAC2的结构与hVDAC1的结构相似,这与最近对zfVDAC2的研究一致。然而,与hVDAC1相比,hVDAC2似乎表现出更高的构象异质性,这反映在更宽的固态核磁共振谱和不太明确的电生理学图谱中。