Structural and functional characterization of Solanum tuberosum VDAC36.

[en] 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.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Lopes-Rodrigues, Maximilien

Matagne, André ; Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines

Zanuy, David

Alemán, Carlos

Perpète, Eric A.

Michaux, Catherine

Language :

English

Title :

Structural and functional characterization of Solanum tuberosum VDAC36.

Publication date :

2020

Journal title :

Proteins

ISSN :

0887-3585

eISSN :

1097-0134

Publisher :

Wiley-Liss Inc, United States - New York

Volume :

Issue :

Pages :

729-739

Peer reviewed :

Peer Reviewed verified by ORBi

Commentary :

Available on ORBi :

since 05 July 2020

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