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Three-dimensional solution structure, dynamics and binding of thioredoxin m from Pisum sativum
dc.contributor.author | Neira, José Luis | |
dc.contributor.author | Palomino Schätzlein, Martina | |
dc.contributor.author | Rejas, Virginia | |
dc.contributor.author | Traverso Gutiérrez, José Ángel | |
dc.contributor.author | Rico, Manual | |
dc.contributor.author | López Gorgé, Julio | |
dc.contributor.author | Chueca, Ana | |
dc.contributor.author | Cámara-Artigas, Ana | |
dc.date.accessioned | 2024-05-28T07:13:50Z | |
dc.date.available | 2024-05-28T07:13:50Z | |
dc.date.issued | 2024-02-01 | |
dc.identifier.citation | Neira, José L., et al. Three-dimensional solution structure, dynamics and binding of thioredoxin m from Pisum sativum. International Journal of Biological Macromolecules 262 (2024) 129781 [10.1016/j.ijbiomac.2024.129781] | es_ES |
dc.identifier.uri | https://hdl.handle.net/10481/92132 | |
dc.description.abstract | Thioredoxins (TRXs) are ubiquitous small, globular proteins involved in cell redox processes. In this work, we report the solution structure of TRX m from Pisum sativum (pea), which has been determined on the basis of 1444 nuclear Overhauser effect- (NOE-) derived distance constraints. The average pairwise root-mean-square deviation (RMSD) for the 20 best structures for the backbone residues (Val7-Glu102) was 1.42 ± 0.15 Å, and 1.97 ± 0.15 Å when all heavy atoms were considered. The structure corresponds to the typical fold of TRXs, with a central five-stranded β-sheet flanked by four α-helices. Some residues had an important exchange dynamic contribution: those around the active site; at the C terminus of β-strand 3; and in the loop preceding α-helix 4. Smaller NOE values were observed at the N and C-terminal residues forming the elements of the secondary structure or, alternatively, in the residues belonging to the loops between those elements. A peptide derived from pea fructose-1,6-biphosphatase (FBPase), comprising the preceding region to the regulatory sequence of FBPase (residues Glu152 to Gln179), was bound to TRX m with an affinity in the low micromolar range, as measured by fluorescence and NMR titration experiments. Upon peptide addition, the intensities of the cross-peaks of all the residues of TRX m were affected, as shown by NMR. The value of the dissociation constant of the peptide from TRX m was larger than that of the intact FBPase, indicating that there are additional factors in other regions of the polypeptide chain of the latter protein affecting the binding to thioredoxin. | es_ES |
dc.description.sponsorship | Consellería de Innovación, Universidades, Ciencia y Sociedad Digital (Generalitat Valenciana) [CIAICO 2021/0135] | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Elsevier | es_ES |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Thioredoxin | es_ES |
dc.subject | Protein-protein interactions | es_ES |
dc.subject | NMR | es_ES |
dc.title | Three-dimensional solution structure, dynamics and binding of thioredoxin m from Pisum sativum | es_ES |
dc.type | journal article | es_ES |
dc.rights.accessRights | open access | es_ES |
dc.identifier.doi | 10.1016/j.ijbiomac.2024.129781 | |
dc.type.hasVersion | VoR | es_ES |