Structural and functional characterization of Solanum tuberosum VDAC36
| Autor: | Maximilien Lopes-Rodrigues, Eric A. Perpète, Carlos Alemán, David Zanuy, André Matagne, Catherine Michaux |
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| Přispěvatelé: | Universitat Politècnica de Catalunya. Departament d'Enginyeria Química, Universitat Politècnica de Catalunya. IMEM-BRT- Innovation in Materials and Molecular Engineering - Biomaterials for Regenerative Therapies |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical Circular dichroism Molecular model Gene Expression voltage-dependent anion channel Biochemistry Protein Refolding Protein structure Adenosine Triphosphate Structural Biology Protein Isoforms Voltage-Dependent Anion Channels Cloning Molecular Plant Proteins 0303 health sciences biology Chemistry 030302 biochemistry & molecular biology Recombinant Proteins Cross-Linking Reagents Phosphatidylcholines Bacterial outer membrane Protein Binding Voltage-dependent anion channel Genetic Vectors ATP binding 03 medical and health sciences Biomolècules Enginyeria química [Àrees temàtiques de la UPC] Escherichia coli Protein Interaction Domains and Motifs protein structure Molecular Biology 030304 developmental biology Solanum tuberosum oligomeric states Binding Sites Osmolar Concentration Protein tertiary structure Protein Structure Tertiary circular dichroism Kinetics Docking (molecular) Liposomes biology.protein Biophysics Protein Conformation beta-Strand Protein Multimerization |
| Zdroj: | UPCommons. Portal del coneixement obert de la UPC Universitat Politècnica de Catalunya (UPC) |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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