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Structural and functional characterization of Solanum tuberosum VDAC36
Author(s) -
LopesRodrigues Maximilien,
Matagne André,
Zanuy David,
Alemán Carlos,
Perpète Eric A.,
Michaux Catherine
Publication year - 2020
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25861
Subject(s) - voltage dependent anion channel , solanum tuberosum , circular dichroism , biophysics , monomer , chemistry , gene isoform , docking (animal) , biochemistry , stereochemistry , bacterial outer membrane , crystallography , biology , polymer , gene , botany , medicine , nursing , organic chemistry , escherichia coli
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.