文章基本信息

标题：The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating
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作者：Rachna Ujwal ; Duilio Cascio ; Jacques-Philippe Colletier 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2008
卷号：105
期号：46
页码：17742-17747
DOI：10.1073/pnas.0809634105
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The voltage-dependent anion channel (VDAC) constitutes the major pathway for the entry and exit of metabolites across the outer membrane of the mitochondria and can serve as a scaffold for molecules that modulate the organelle. We report the crystal structure of a {beta}-barrel eukaryotic membrane protein, the murine VDAC1 (mVDAC1) at 2.3 A resolution, revealing a high-resolution image of its architecture formed by 19 {beta}-strands. Unlike the recent NMR structure of human VDAC1, the position of the voltage-sensing N-terminal segment is clearly resolved. The {alpha}-helix of the N-terminal segment is oriented against the interior wall, causing a partial narrowing at the center of the pore. This segment is ideally positioned to regulate the conductance of ions and metabolites passing through the VDAC pore.
关键词：β-barrel ; mitochondria ; outer membrane protein ; ATP flux