Three-dimensional solution structure, dynamics and binding of thioredoxin m from Pisum sativum
Metadatos
Mostrar el registro completo del ítemAutor
Neira, José Luis; Palomino Schätzlein, Martina; Rejas, Virginia; Traverso Gutiérrez, José Ángel; Rico, Manual; López Gorgé, Julio; Chueca, Ana; Cámara-Artigas, AnaEditorial
Elsevier
Materia
Thioredoxin Protein-protein interactions NMR
Fecha
2024-02-01Referencia bibliográfica
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]
Patrocinador
Consellería de Innovación, Universidades, Ciencia y Sociedad Digital (Generalitat Valenciana) [CIAICO 2021/0135]Resumen
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.