Structural and functional characterization of Solanum tuberosum VDAC36

Maximilien Lopes-Rodrigues, André Matagne, David Zanuy, Carlos Alemán, Eric A. Perpète, Catherine Michaux

Research output: Contribution to journalArticlepeer-review


As it forms water-filled channel in the mitochondria outer membrane and diffuses essential metabolites such as NADH and ATP, the voltage-dependent anion channel (VDAC) protein family plays a central role in all eukaryotic cells. In comparison with their mammalian homologues, little is known about the structural and functional properties of plant VDACs. In the present contribution, one of the two VDACs isoforms of Solanum tuberosum, stVDAC36, has been successfully overexpressed and refolded by an in-house method, as demonstrated by the information on its secondary and tertiary structure gathered from circular dichroism and intrinsic fluorescence. Cross-linking and molecular modeling studies have evidenced the presence of dimers and tetramers, and they suggest the formation of an intermolecular disulfide bond between two stVDAC36 monomers. The pore-forming activity was also assessed by liposome swelling assays, indicating a typical pore diameter between 2.0 and 2.7 nm. Finally, insights about the ATP binding inside the pore are given by docking studies and electrostatic calculations.

Original languageEnglish
Pages (from-to)729-739
Number of pages11
JournalProteins: Structure, Function and Bioinformatics
Issue number6
Early online date2019
Publication statusPublished - 1 Jun 2020


  • ATP binding
  • circular dichroism
  • oligomeric states
  • protein structure
  • voltage-dependent anion channel


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