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Structure of the human voltage-dependent anion channel

2008

Article

ei


The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitochondrially induced apoptosis. Here, we present the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography. Human VDAC1 (hVDAC1) adopts a β-barrel architecture composed of 19 β-strands with an α-helix located horizontally midway within the pore. Bioinformatic analysis indicates that this channel architecture is common to all VDAC proteins and is adopted by the general import pore TOM40 of mammals, which is also located in the MOM.

Author(s): Bayrhuber, M. and Meins, T. and Habeck, M. and Becker, S. and Giller, K. and Villinger, S. and Vonrhein, C. and Griesinger, C. and Zweckstetter, M. and Zeth, K.
Journal: Proceedings of the National Academy of Sciences of the United States of America
Volume: 105
Number (issue): 40
Pages: 15370-15375
Year: 2008
Month: October
Day: 0

Department(s): Empirical Inference
Bibtex Type: Article (article)

Digital: 0
DOI: 10.1073/pnas.0808115105
Language: en
Organization: Max-Planck-Gesellschaft
School: Biologische Kybernetik

Links: Web

BibTex

@article{5523,
  title = {Structure of the human voltage-dependent anion channel},
  author = {Bayrhuber, M. and Meins, T. and Habeck, M. and Becker, S. and Giller, K. and Villinger, S. and Vonrhein, C. and Griesinger, C. and Zweckstetter, M. and Zeth, K.},
  journal = {Proceedings of the National Academy of Sciences of the United States of America},
  volume = {105},
  number = {40},
  pages = {15370-15375},
  organization = {Max-Planck-Gesellschaft},
  school = {Biologische Kybernetik},
  month = oct,
  year = {2008},
  month_numeric = {10}
}