Mostrar el registro sencillo del ítem

Study of the structure and binding site features of FaEXPA2, an α-expansin protein involved in strawberry fruit softening

dc.contributor.authorValenzuela-Riffo F.
dc.contributor.authorMorales-Quintana L.
dc.date.accessioned2020-09-02T22:29:54Z
dc.date.available2020-09-02T22:29:54Z
dc.date.issued2020
dc.identifier10.1016/j.compbiolchem.2020.107279
dc.identifier.citation87, , -
dc.identifier.issn14769271
dc.identifier.urihttps://hdl.handle.net/20.500.12728/6508
dc.descriptionTissue softening accompanies the ripening of many fruits and initiates the processes of irreversible deterioration. Expansins are plant cell wall proteins that have been proposed to disrupt hydrogen bonds within the cell wall polymer matrix. Several authors have shown that FaEXPA2 is a key gene that shows an increased expression level during ripening and softening of the strawberry fruit. For this reason, FaEXPA2 is frequently used as a molecular marker of softening in strawberry fruit, and changes in its relative expression have been related to changes in fruit firmness. In this context, we previously reported that FaEXPA2 has a high accumulation rate during fruit ripening in four different strawberry cultivars; however, the molecular mechanism of FaEXPA2 or expansins in general is not yet clear. Herein, a 3D model of the FaEXPA2 protein was built by comparative modeling to understand how FaEXPA2 interacts with different cell wall components at the molecular level. First, the structure was shown to display two domains characteristic of the other expansins that were previously described. The protein-ligand interaction was evaluated by molecular dynamic (MD) simulation using four different long ligands (a cellulose fiber, two of the more important xyloglucan (XG) fibers found in strawberry (XXXG and XXFG type), and a pectin (homogalacturonic acid type)). The results showed that FaEXPA2 formed a more stable complex with cellulose than other ligands via the different residues present in the open groove surface of its two domains, while FaEXPA2 did not interact with the pectin ligand. © 2020 Elsevier Ltd
dc.language.isoen
dc.publisherElsevier Ltd
dc.subjectExpansin protein
dc.subjectFruit softening
dc.subjectMolecular dynamic simulation
dc.subjectProtein-ligand interaction
dc.subjectStrawberry
dc.subject3D modeling
dc.subjectCellulose
dc.subjectDeterioration
dc.subjectHydrogen bonds
dc.subjectLigands
dc.subjectMolecular dynamics
dc.subjectPlants (botany)
dc.subjectProteins
dc.subjectWalls (structural partitions)
dc.subjectAccumulation rates
dc.subjectCell wall polymers
dc.subjectCell-wall components
dc.subjectComparative modeling
dc.subjectMolecular mechanism
dc.subjectProtein-ligand interactions
dc.subjectRipening and softening
dc.subjectStrawberry cultivars
dc.subjectFruits
dc.subjectCellulose
dc.subjectDegradation
dc.subjectFruits
dc.subjectHydrogen Bonds
dc.subjectLigands
dc.subjectProteins
dc.titleStudy of the structure and binding site features of FaEXPA2, an α-expansin protein involved in strawberry fruit softening
dc.typeArticle


Ficheros en el ítem

Thumbnail
Nombre:
item_2-s2.0-85085739583.pdf
Tamaño:
3.006Kb
Formato:
PDF
Ver/

Este ítem aparece en la(s) siguiente(s) colección(ones)

Mostrar el registro sencillo del ítem