(1)H, (13)C and (15)N resonance assignment of the mature form of monothiol glutaredoxin 1 from the pathogen Trypanosoma brucei.
Glutaredoxins (Grx) are small proteins, conserved throughout all the kingdoms of life, which are engaged in a wide variety of biological processes. According to the number of cysteines in their active site, Grx are classified as dithiolic or monothiolic (1-C-Grx). In most organisms, 1-C-Grx are implicated in iron-sulfur cluster (FeS) metabolism and utilize glutathione as cofactor. Trypanosomatids are parasitic protozoa of the order Kinetoplastida, which cause severe diseases in humans and domestic animals. These parasites exploit a unique thiol-dependent redox system based on bis(glutathionyl)spermidine (trypanothione) rather than on glutathione. Mitochondrial 1-C-Grx1 from trypanosomes differs from orthologues in several features including the use of trypanothione as ligand for FeS binding and the presence of a parasite-specific N-terminal extension. We have recently shown that 1-C-Grx1 from Trypanosoma brucei is indispensable for parasite survival in mouse, making this protein a potential drug target candidate against trypanosomiasis. However, structural information for the full-length form of 1-C-Grx1 is still lacking. Here, we report the NMR resonance assignment of the mature form of Tb1-C-Grx1 including an N-terminal tail, paving the way to disclose the role of this intrinsically disordered region in the protein function.
Department of Chemical Sciences, University of Padova, Via Marzolo 1, 35131, Padova, Italy.
Mattia
M
Sturlese
Moreno
M
Lelli
Bruno
B
Manta
Stefano
S
Mammi
Marcelo A
MA
Comini
Massimo
M
Bellanda
D054477:Glutaredoxins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D014346:Trypanosoma brucei brucei / Q000201:enzymology*
D054477:Glutaredoxins