Structural and functional characterization of Solanum tuberosum VDAC36.

Autor:	Lopes-Rodrigues M; Laboratoire de Chimie Physique des Biomolécules, Unité de Chimie Physique Théorique et Structurale (UCPTS), University of Namur, Namur, Belgium.; Namur Institute of Structured Matter, University of Namur, Namur, Belgium.; Departament d'Enginyeria Química, EEBE, Universitat Politècnica de Catalunya, C/Eduard Maristany, Barcelona, Spain.; Barcelona Research Center for Multiscale Science and Engineering, Universitat Politècnica de Catalunya, Eduard Maristany, Barcelona, Spain., Matagne A; Laboratoire d'Enzymologie et Repliement des Protéines, Centre d'Ingénierie des Protéines (CIP), Université de Liège, Liège, Belgium., Zanuy D; Departament d'Enginyeria Química, EEBE, Universitat Politècnica de Catalunya, C/Eduard Maristany, Barcelona, Spain., Alemán C; Departament d'Enginyeria Química, EEBE, Universitat Politècnica de Catalunya, C/Eduard Maristany, Barcelona, Spain.; Barcelona Research Center for Multiscale Science and Engineering, Universitat Politècnica de Catalunya, Eduard Maristany, Barcelona, Spain., Perpète EA; Laboratoire de Chimie Physique des Biomolécules, Unité de Chimie Physique Théorique et Structurale (UCPTS), University of Namur, Namur, Belgium.; Namur Institute of Structured Matter, University of Namur, Namur, Belgium.; Namur Research Institute for Life Sciences, University of Namur, Namur, Belgium., Michaux C; Laboratoire de Chimie Physique des Biomolécules, Unité de Chimie Physique Théorique et Structurale (UCPTS), University of Namur, Namur, Belgium.; Namur Institute of Structured Matter, University of Namur, Namur, Belgium.; Institute of Life-Earth-Environment, University of Namur, Namur, Belgium.
Jazyk:	angličtina
Zdroj:	Proteins [Proteins] 2020 Jun; Vol. 88 (6), pp. 729-739. Date of Electronic Publication: 2019 Dec 20.
DOI:	10.1002/prot.25861
Abstrakt:	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. (© 2019 Wiley Periodicals, Inc.)
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu Plný text