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2N84

Solution structure of the FHA domain of TbPar42

Summary for 2N84
Entry DOI10.2210/pdb2n84/pdb
Related2N87
NMR InformationBMRB: 25834
DescriptorUncharacterized protein (1 entity in total)
Functional Keywordsfha domain, parvulin, isomerase
Biological sourceTrypanosoma brucei brucei TREU927
Total number of polymer chains1
Total formula weight19288.42
Authors
Rehic, E.,Bayer, P. (deposition date: 2015-10-04, release date: 2016-10-12, Last modification date: 2024-05-15)
Primary citationRehic, 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, 9:-, 2019
Cited by
PubMed Abstract: is a unicellular eukaryotic parasite, which causes the African sleeping sickness in humans. The recently discovered trypanosomal protein Parvulin 42 (Par42) plays a key role in parasite cell proliferation. Homologues of this two-domain protein are exclusively found in protozoa species. Par42 exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl--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 Par42, discuss their intra-molecular interplay, and give some initial hints as to potential cellular functions of the protein.
PubMed: 30866577
DOI: 10.3390/biom9030093
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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