Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei

Rehic, Edisa GND; Hönig, Dana GND; Kamba, Bianca E. GND; Göhring, Anna GND; Hofmann, Eckhard GND; Gasper, Raphael ORCID; Matena, Anja GND; Bayer, Peter GND

Trypanosoma brucei is a unicellular eukaryotic parasite, which causes the African sleeping sickness in humans. The recently discovered trypanosomal protein Parvulin 42 (TbPar42) plays a key role in parasite cell proliferation. Homologues of this two-domain protein are exclusively found in protozoa species. TbPar42 exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Using NMR and X-ray analysis as well as activity assays, we report on the structures of the single domains of TbPar42, discuss their intra-molecular interplay, and give some initial hints as to potential cellular functions of the protein.

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Rehic, E., Hönig, D., Kamba, B.E., Göhring, A., Hofmann, E., Gasper, R., Matena, A., Bayer, P., 2019. Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei. https://doi.org/10.3390/biom9030093
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