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Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei.

ABSTRACT: 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.

SUBMITTER: Rehic E

PROVIDER: S-EPMC6468809 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

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Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei.

Rehic Edisa E Hoenig Dana D Kamba Bianca E BE Goehring Anna A Hofmann Eckhard E Gasper Raphael R Matena Anja A Bayer Peter P

Biomolecules 20190307 3

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 ...[more]

PMID: 30866577

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