Structural highlights
Function
Q57XM6_TRYB2
Publication Abstract from PubMed
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.
Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei.,Rehic E, Hoenig D, Kamba BE, Goehring A, Hofmann E, Gasper R, Matena A, Bayer P Biomolecules. 2019 Mar 7;9(3). pii: biom9030093. doi: 10.3390/biom9030093. PMID:30866577[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rehic E, Hoenig D, Kamba BE, Goehring A, Hofmann E, Gasper R, Matena A, Bayer P. Structural Analysis of the 42 kDa Parvulin of Trypanosoma brucei. Biomolecules. 2019 Mar 7;9(3). pii: biom9030093. doi: 10.3390/biom9030093. PMID:30866577 doi:http://dx.doi.org/10.3390/biom9030093
