ArticleThe Journal of membrane biology2007
High-level expression, refolding and probing the natural fold of the human voltage-dependent anion channel isoforms I and II.
Article in The Journal of membrane biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 50 citations in OpenAlex.
- Solute Transport through Mitochondrial Porins In Vitro and In Vivo.Biomolecules · 2024Review
- Strategies for Successful Over-Expression of Human Membrane Transport Systems Using Bacterial Hosts: Future Perspectives.International journal of molecular sciences · 2022Review
- Historical Perspective of Pore-Forming Activity Studies of Voltage-Dependent Anion Channel (Eukaryotic or Mitochondrial Porin) Since Its Discovery in the 70th of the Last Century.Frontiers in physiology · 2021Review
- Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions.Frontiers in physiology · 2021Review
- Crystal structural characterization reveals novel oligomeric interactions of human voltage-dependent anion channel 1.Protein science : a publication of the Protein Society · 2017Article
- Voltage Dependence of Conformational Dynamics and Subconducting States of VDAC-1.Biophysical journal · 2016Article
- Molecular Plasticity of the Human Voltage-Dependent Anion Channel Embedded Into a Membrane.Structure (London, England : 1993) · 2016Article
- Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.Journal of biomolecular NMR · 2015Article
- High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population.The Journal of biological chemistry · 2014Article
- Tyrosine nitration of voltage-dependent anion channels in cardiac ischemia-reperfusion: reduction by peroxynitrite scavenging.Biochimica et biophysica acta · 2012Article
- β-Barrel mobility underlies closure of the voltage-dependent anion channel.Structure (London, England : 1993) · 2012Article
- Protein translocation through Tom40: kinetics of peptide release.Biophysical journal · 2012Article
- Article
- Functional refolding and characterization of two Tom40 isoforms from human mitochondria.The Journal of membrane biology · 2011Article
- The 3D structures of VDAC represent a native conformation.Trends in biochemical sciences · 2010Review
- Phosphorylation by Nek1 regulates opening and closing of voltage dependent anion channel 1.Biochemical and biophysical research communications · 2010Article
- Tuning microbial hosts for membrane protein production.Microbial cell factories · 2009Review
- The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins.Current opinion in structural biology · 2009Review
- The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Structure of the human voltage-dependent anion channel.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The voltage-dependent anion channel (VDAC) is the major protein found in the outer membrane of mitochondria. The channel is responsible for the exchange of ATP/ADP and the translocation of ions and other small metabolites over the membrane. In order to obtain large amounts of pure and suitably folded human VDAC for functional and structural studies, the genes of the human isoforms I and II (HVDAC1 and HVDAC2) were cloned in Escherichia coli. High-level expression led to inclusion body formation. Both proteins could be refolded in vitro by adding denatured protein to a solution of zwitterionic or nonionic detergents. A highly efficient and fast protocol for refolding was developed that yielded more than 50 mg of pure human VDACs per liter of cell culture. The native and functional state of the refolded porins was probed by Fourier transform infrared spectroscopy to determine the secondary structure composition and by electrophysiological measurements, demonstrating the pore-forming activity of HVDAC1. Furthermore, binding of HVDAC1 to immobilized ATP was demonstrated. Limited proteolysis of HVDAC1 protein embedded in detergent micelles in combination with matrix-assisted laser desorption ionization mass spectrometric analysis was applied to identify micelle-exposed regions of the protein and to develop an improved topology model. Our analysis strongly suggests a 16-stranded, antiparallel beta-barrel with one large and seven short loops and turns. Initial crystallization trials of the protein yielded crystals diffracting to 8 Angstrom resolution.
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