NMR assignments of oxidised thioredoxin from Plasmodium falciparum.
During its life cycle, the malaria parasite Plasmodium falciparum is found intracellular to human erythrocytes, where its survival and ability to multiply critically depends on the control of the environment redox state. Thioredoxin is a small protein containing 104 amino acids that is part of the parasite specific redox system. During the catalytic cycle it alternates between a reduced and oxidised form. Here we report the complete resonance assignment of Plasmodium falciparum thioredoxin in its oxidized form by heteronuclear multidimensional spectroscopy. The obtained chemical shifts differ significantly from those reported earlier for this protein in its reduced state.
Munte
Claudia Elisabeth
CE
Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Universitätsstr. 31, 93040, Regensburg, Germany. claudia.munte@biologie.uni-regensburg.de
Becker
Katja
K
Schirmer
Rolf Heiner
RH
Kalbitzer
Hans Robert
HR
D000818:Animals; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D010963:Plasmodium falciparum / Q000737:chemistry*; D015800:Protozoan Proteins / Q000737:chemistry* / Q000378:metabolism; D013879:Thioredoxins / Q000737:chemistry* / Q000378:metabolism
D015800:Protozoan Proteins; D013879:Thioredoxins