Affiliation:
1. Departamento de Genética Universidade Federal do Rio Grande do Sul Porto Alegre Rio Grande do Sul Brazil
2. Laboratório de Tecnologia Biomolecular Instituto de Ciências Biológicas, Universidade Federal do Pará Belém Pará Brazil
Abstract
AbstractIntrinsically disordered proteins (IDPs) have numerous dynamic conformations. Given the difficulties in tracking temporarily folded states of this kind of protein, methods such as molecular modeling and molecular dynamics (MD) simulations make the process less costly, less laborious, and more detailed. Few plant IDPs have been characterized so far, such as proteins from the Abscisic acid, Stress and Ripening (ASR) family. The present work applied, for the first time, the two above‐mentioned tools to test the feasibility of determining a three‐dimensional transition model of OsASR5 and to investigate the relationship between OsASR5 and zinc. We found that one of OsASR5's conformers contains α‐helices, turns, and loops and that the metal binding resulted in a predominance of α‐helix. This stability is possibly imperative for the transcription factor activity. The promoter region of a sugar transporter was chosen to test this hypothesis and free energy calculations showed how the ion is mandatory for this complex formation. The results produced here aim to clarify which conformation the protein in the bound state assumes and which residues are involved in the process, besides developing the understanding of how the flexibility of these proteins can contribute to the response to environmental stresses.
Funder
Conselho Nacional de Desenvolvimento Científico e Tecnológico
Subject
Molecular Biology,Biochemistry,Structural Biology
Cited by
1 articles.
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