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Biomolecules 2019, 9(3), 93;

Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei

University Duisburg-Essen, Research Group Structural and Medicinal Biochemistry, Centre for Medical Biotechnology (ZMB), University of Duisburg-Essen, 45117 Essen, Germany
Protein Crystallography, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44801 Bochum, Germany
Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany
Author to whom correspondence should be addressed.
Received: 19 February 2019 / Revised: 28 February 2019 / Accepted: 28 February 2019 / Published: 7 March 2019
(This article belongs to the Section Molecular Structure and Dynamics)
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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. View Full-Text
Keywords: Trypanosoma brucei; Parvulin; cis/trans Isomerase; PPIase; FHA Trypanosoma brucei; Parvulin; cis/trans Isomerase; PPIase; FHA

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Rehic, E.; Hoenig, D.; Kamba, B.E.; Goehring, A.; Hofmann, E.; Gasper, R.; Matena, A.; Bayer, P. Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei. Biomolecules 2019, 9, 93.

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